Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: alkaline phosphatase

Gene: phoA Accession Numbers: EG10727 (MetaCyc), b0383, ECK0378

Synonyms: psiA

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of alkaline phosphatase = [PhoA]2

Summary:
Alkaline phosphatase is a periplasmic, homodimeric enzyme that catalyses the hydrolysis and transphosphorylation of a wide variety of phosphate monoesters [Torriani60, Heppel62, Malamy61, Chang80a]. The reaction proceeds through a phosphoseryl intermediate with the subsequent release of inorganic phosphate and alcohol [Schwartz61, Holtz99, Stec98, Stec00]. The transphosphorylation reaction results in the transfer of a phosphoryl group to the alcohol of acceptors such as Tris or ethanolamine [Dayan64, Wilson64a] . Alkaline phosphatase is a metalloenzyme, binding two zinc atoms and one magnesium ion per monomer [Plocke62, Plocke62a, Sowadski85, Janeway93].

The amount of alkaline phosphatase is optimal when cells are starved for phosphate - which is the most common environment for E.coli in the human gut - and is much reduced when there is an excess of phosphate [Torriani60]. Under conditions of limiting phosphate, alkaline phosphatase accounts for approximately 6% of the total protein synthesized [Garen60]

Alkaline phosphatase occurs in three major forms designated isozymes 1, 2 and 3 whose relative proprotions are dependent on the growth conditions [Kelley73, Schlesinger68]. The isozymes are differentiated by the presence or absence of an NH2-terminal arginine residue: present in both subunits of isozyme 1, absent in both subunits of isozyme 3 and heterogenous in isozyme 2 [Nakata78, Bradshaw81]. Removal of the N-terminal arginine is catalysed by the membrane-associated, proteolytic enyzyme Iap [Nakata77, Nakata84].

The precursor polypeptide is secreted across the inner membrane to the periplasmic space concommitant with removal of the signal sequence [Chang86a]. Folding of PhoA in vivo is catalysed by the periplasmic protein, DsbA and is thought to occur as the polypeptide elongates from the ribosome [Kadokura09].

phoA is part of the phosphate regulon; its expression is positively regulated by the PhoB transcriptional regulator [Makino86]

A single report has also suggested that the PhoA protein oxidizes phosphite to phosphate, producing molecular H2 [Yang04a].

Reviews: [Coleman92, Holtz99, Stigbrand82, Torriani90].

Citations: [Horiuchi59, Nesmeyanova81, Applebury70, Ma95a, Ma96a, Le02a, Michaelis83, Inouye77, Torriani68, Schlesinger68a]

Gene Citations: [Kikuchi81]

Locations: periplasmic space

Map Position: [400,971 -> 402,386]

Molecular Weight of Polypeptide: 49.439 kD (from nucleotide sequence)

pI: 6.09

Unification Links: ASAP:ABE-0001328 , CGSC:398 , DIP:DIP-10496N , EchoBASE:EB0720 , EcoGene:EG10727 , EcoliWiki:b0383 , Mint:MINT-1283619 , ModBase:P00634 , OU-Microarray:b0383 , PortEco:phoA , PR:PRO_000023540 , Protein Model Portal:P00634 , RefSeq:NP_414917 , RegulonDB:EG10727 , SMR:P00634 , String:511145.b0383 , UniProt:P00634

Relationship Links: InterPro:IN-FAMILY:IPR001952 , InterPro:IN-FAMILY:IPR017849 , InterPro:IN-FAMILY:IPR017850 , InterPro:IN-FAMILY:IPR018299 , PDB:Structure:1AJA , PDB:Structure:1AJB , PDB:Structure:1AJC , PDB:Structure:1AJD , PDB:Structure:1ALH , PDB:Structure:1ALI , PDB:Structure:1ALJ , PDB:Structure:1ALK , PDB:Structure:1ANI , PDB:Structure:1ANJ , PDB:Structure:1B8J , PDB:Structure:1ED8 , PDB:Structure:1ED9 , PDB:Structure:1ELX , PDB:Structure:1ELY , PDB:Structure:1ELZ , PDB:Structure:1EW8 , PDB:Structure:1EW9 , PDB:Structure:1HJK , PDB:Structure:1HQA , PDB:Structure:1KH4 , PDB:Structure:1KH5 , PDB:Structure:1KH7 , PDB:Structure:1KH9 , PDB:Structure:1KHJ , PDB:Structure:1KHK , PDB:Structure:1KHL , PDB:Structure:1KHN , PDB:Structure:1URA , PDB:Structure:1URB , PDB:Structure:1Y6V , PDB:Structure:1Y7A , PDB:Structure:2ANH , PDB:Structure:2G9Y , PDB:Structure:2GA3 , PDB:Structure:3BDF , PDB:Structure:3BDG , PDB:Structure:3BDH , PDB:Structure:3CMR , PDB:Structure:3DPC , PDB:Structure:3DYC , PDB:Structure:3TG0 , PDB:Structure:4KM4 , Pfam:IN-FAMILY:PF00245 , Prints:IN-FAMILY:PR00113 , Prosite:IN-FAMILY:PS00123 , Smart:IN-FAMILY:SM00098

Gene-Reaction Schematic: ?

Instance reaction of [a phosphate monoester + H2O → an alcohol + phosphate] (3.1.3.1):
i1: ethylphosphate + H2O → ethanol + phosphate (3.1.3.1)

Instance reactions of [D-glucopyranose 6-phosphate + H2O → D-glucopyranose + phosphate] (3.1.3.9/3.1.3.58):
i2: α-D-glucose 6-phosphate + H2O → α-D-glucose + phosphate (3.1.3.9/3.1.3.58)

i3: β-D-glucose 6-phosphate + H2O → β-D-glucose + phosphate (3.1.3.9/3.1.3.58)

GO Terms:

Biological Process: GO:0016311 - dephosphorylation Inferred from experiment [Garen60]
GO:0055114 - oxidation-reduction process Inferred from experiment [Yang04a]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
Molecular Function: GO:0000287 - magnesium ion binding Inferred from experiment [Sowadski85]
GO:0004035 - alkaline phosphatase activity Inferred from experiment Inferred by computational analysis [GOA01, Garen60]
GO:0005515 - protein binding Inferred from experiment [Kadokura09]
GO:0008270 - zinc ion binding Inferred from experiment [Plocke62a, Sowadski85]
GO:0030613 - oxidoreductase activity, acting on phosphorus or arsenic in donors Inferred from experiment [Yang04a]
GO:0033748 - hydrogenase (acceptor) activity Inferred from experiment [Yang04a]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016791 - phosphatase activity Inferred by computational analysis [GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space Inferred from experiment Inferred by computational analysis [DiazMejia09, Malamy64]
GO:0042597 - periplasmic space Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, Malamy64]

MultiFun Terms: metabolism metabolism of other compounds phosphorous metabolism

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: alkaline phosphatase

Synonyms: APase, AP, alkaline phosphomonesterase, glycerophosphatase, orthophosphoric-monoester phosphohydrolase (alkaline optimum)

EC Number: 3.1.3.1

a phosphate monoester[periplasmic space] + H2O[periplasmic space] <=> an alcohol[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Alternative Substrates for a phosphate monoester: ATP [Heppel62 ] , dATP [Heppel62 ] , UDP [Heppel62 ] , dGTP [Heppel62 ] , dTTP [Heppel62 ] , dCTP [Heppel62 ]

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Cofactors or Prosthetic Groups: Mg2+ [Sowadski85], Zn2+ [Sowadski85]

Inhibitors (Competitive): phosphate [Kim91] , arsenate [Sowadski85] , thioglycolate [Malamy64a] , vanadate [Stankiewicz88] , chromate [Stankiewicz88] , molybdate [Stankiewicz88]

Inhibitors (Unknown Mechanism): L-cysteine [Malamy64a]

pH(opt): 8.0 [Garen60]


Enzymatic reaction of: β-D-glucose 6-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.9/3.1.3.58

β-D-glucose 6-phosphate + H2O <=> β-D-glucose + phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Credits:
Imported from MetaCyc 04-Feb-2014 by Caspi R , SRI International
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: α-D-glucose 6-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.9/3.1.3.58

α-D-glucose 6-phosphate + H2O <=> α-D-glucose + phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Credits:
Imported from MetaCyc 04-Feb-2014 by Caspi R , SRI International
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: diphosphate phosphatase (alkaline phosphatase)

EC Number: 3.6.1.1

diphosphate[periplasmic space] + H2O[periplasmic space] <=> 2 phosphate[periplasmic space] + H+[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: triphosphate phosphatase (alkaline phosphatase)

EC Number: 3.6.1.25

PPPi[periplasmic space] + H2O[periplasmic space] <=> phosphate[periplasmic space] + diphosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 3-phospho-L-serine phosphatase (alkaline phosphatase)

3-phospho-L-serine[periplasmic space] + H2O[periplasmic space] <=> L-serine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: L-threonine O-3-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

L-threonine 3-O-phosphate[periplasmic space] + H2O[periplasmic space] <=> L-threonine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: ribose 5-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

D-ribose 5-phosphate[periplasmic space] + H2O[periplasmic space] <=> aldehydo-D-ribose[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: glucose-1-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.10

α-D-glucose 1-phosphate[periplasmic space] + H2O[periplasmic space] <=> D-glucopyranose[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: glucose-6-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.9/3.1.3.58

D-glucopyranose 6-phosphate[periplasmic space] + H2O[periplasmic space] <=> D-glucopyranose[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: glycerol-2-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.19

glycerol 2-phosphate[periplasmic space] + H2O[periplasmic space] <=> glycerol[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: phosphoglycerate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.20

2-phospho-D-glycerate[periplasmic space] + H2O[periplasmic space] <=> D-glycerate[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: fructose-1,6-biphosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.11

fructose 1,6-bisphosphate[periplasmic space] + H2O[periplasmic space] <=> β-D-fructofuranose 6-phosphate[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

In Pathways: photosynthetic 3-hydroxybutyrate biosynthesis (engineered) , superpathway of hexitol degradation (bacteria) , superpathway of N-acetylneuraminate degradation , glycolysis II (from fructose 6-phosphate)

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: NADP+ phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

NADP+[periplasmic space] + H2O[periplasmic space] <=> NAD+[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: FMN phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

FMN[periplasmic space] + H2O[periplasmic space] <=> riboflavin[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: L-histidinol-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.15

L-histidinol-phosphate[periplasmic space] + H2O[periplasmic space] <=> histidinol[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: phosphoenolpyruvate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.60

phosphoenolpyruvate[periplasmic space] + H2O[periplasmic space] <=> pyruvate[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: AMP phosphatase (alkaline phosphatase)

AMP[periplasmic space] + H2O[periplasmic space] <=> adenosine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

In Pathways: purine nucleotides degradation II (aerobic) , adenosine nucleotides degradation II

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: dAMP phosphatase (alkaline phosphatase)

dAMP[periplasmic space] + H2O[periplasmic space] <=> 2'-deoxyadenosine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 3'AMP phosphatase (alkaline phosphatase)

adenosine 3'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> adenosine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 2'AMP phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

adenosine 2'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> adenosine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: dGMP phosphatase (alkaline phosphatase)

dGMP[periplasmic space] + H2O[periplasmic space] <=> 2'-deoxyguanosine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 2'GMP phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

guanosine 2'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> guanosine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 2'CMP phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

cytidine 2'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> cytidine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 3'CMP phosphatase (alkaline phosphatase)

cytidine-3'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> cytidine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: CMP phosphatase (alkaline phosphatase)

CMP[periplasmic space] + H2O[periplasmic space] <=> cytidine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: dCMP phosphatase (alkaline phosphatase)

dCMP[periplasmic space] + H2O[periplasmic space] <=> 2'-deoxycytidine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 2'UMP phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

uridine 2'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> uridine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 3'UMP phosphatase (alkaline phosphatase)

uridine 3'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> uridine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: UMP phosphatase (alkaline phosphatase)

UMP[periplasmic space] + H2O[periplasmic space] <=> uridine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: IMP phosphatase (alkaline phosphatase)

IMP[periplasmic space] + H2O[periplasmic space] <=> inosine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: pyridoxine-5'-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.74

pyridoxine 5'-phosphate[periplasmic space] + H2O[periplasmic space] <=> pyridoxine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: pyridoxal 5'-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.74

pyridoxal 5'-phosphate[periplasmic space] + H2O[periplasmic space] <=> pyridoxal[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 4-nitrophenyl phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.41

4-nitrophenyl phosphate[periplasmic space] + H2O[periplasmic space] <=> 4-nitrophenol[periplasmic space] + phosphate[periplasmic space] + H+[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Note: The enzyme may catalyze this reaction in vitro, but this reaction is not considered to be physiologically relevant.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: cysteamine S-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

cysteamine S-phosphate[periplasmic space] + H2O[periplasmic space] <=> cysteamine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: phosphocholine phosphatase (alkaline phosphatase)

EC Number: 3.1.3.75

phosphocholine[periplasmic space] + H2O[periplasmic space] <=> choline[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: phosphoryl-ethanolamine phosphatase (alkaline phosphatase)

EC Number: 3.1.3.75

phosphoryl-ethanolamine[periplasmic space] + H2O[periplasmic space] <=> ethanolamine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Sequence Features

Feature Class Location Citations Comment
Signal-Sequence 1 -> 21
[UniProt10a]
Sequence-Conflict 10
[Gray85, UniProt11]
Alternate sequence: V; UniProt: (in Ref. 12; AAA23431).
Extrinsic-Sequence-Variant 22
[UniProt10a]
Alternate sequence: missing; UniProt: (in isozyme 3);
Chain 22 -> 471
[UniProt09]
UniProt: Alkaline phosphatase;
Metal-Binding-Site 73
[UniProt10a]
UniProt: Magnesium;
Sequence-Conflict 78 -> 80
[Kikuchi81, UniProt10a]
Alternate sequence: WGS; UniProt: (in Ref. 8; AAA24359);
Active-Site 124
[UniProt10a]
UniProt: Phosphoserine intermediate;
Metal-Binding-Site 175
[UniProt10a]
UniProt: Magnesium;
Metal-Binding-Site 177
[UniProt10a]
UniProt: Magnesium;
Disulfide-Bond-Site 200, 190
[UniProt10a]
Sequence-Conflict 198
[Bradshaw81, UniProt10a]
Alternate sequence: Q; UniProt: (in Ref. 9; AA sequence);
Disulfide-Bond-Site 358, 308
[UniProt10a]
Metal-Binding-Site 344
[UniProt10a]
UniProt: Magnesium;
Metal-Binding-Site 349
[UniProt10a]
UniProt: Zinc 1;
Metal-Binding-Site 353
[UniProt10a]
UniProt: Zinc 1;
Metal-Binding-Site 391
[UniProt10a]
UniProt: Zinc 2;
Metal-Binding-Site 392
[UniProt10a]
UniProt: Zinc 2;
Metal-Binding-Site 434
[UniProt10a]
UniProt: Zinc 1;

History:
10/20/97 Gene b0383 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10727; confirmed by SwissProt match.


References

Applebury70: Applebury ML, Johnson BP, Coleman JE (1970). "Phosphate binding to alkaline phosphatase. Metal ion dependence." J Biol Chem 245(19);4968-76. PMID: 4319108

Bradshaw81: Bradshaw RA, Cancedda F, Ericsson LH, Neumann PA, Piccoli SP, Schlesinger MJ, Shriefer K, Walsh KA (1981). "Amino acid sequence of Escherichia coli alkaline phosphatase." Proc Natl Acad Sci U S A 1981;78(6);3473-7. PMID: 7022451

Chang80a: Chang CN, Inouye H, Model P, Beckwith J (1980). "Processing of alkaline phosphatase precursor to the mature enzyme by an Escherichia coli inner membrane preparation." J Bacteriol 142(2);726-8. PMID: 6991486

Chang86a: Chang CN, Kuang WJ, Chen EY (1986). "Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli." Gene 1986;44(1);121-5. PMID: 3533724

Coleman92: Coleman JE (1992). "Structure and mechanism of alkaline phosphatase." Annu Rev Biophys Biomol Struct 1992;21;441-83. PMID: 1525473

Dayan64: Dayan J, Wilson IB (1964). "The phosphorylation of Tris by alkaline phosphatase." Biochim Biophys Acta 81;620-3. PMID: 14171894

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Garen60: Garen A, Levinthal C (1960). "A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli. I. Purification and characterization of alkaline phosphatase." Biochim Biophys Acta 38;470-83. PMID: 13826559

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Gray85: Gray GL, Baldridge JS, McKeown KS, Heyneker HL, Chang CN (1985). "Periplasmic production of correctly processed human growth hormone in Escherichia coli: natural and bacterial signal sequences are interchangeable." Gene 39(2-3);247-54. PMID: 3912261

Heppel62: Heppel LA, Harkness DR, Hilmoe RJ (1962). "A study of the substrate specificity and other properties of the alkaline phosphatase of Escherichia coli." J Biol Chem 237;841-6. PMID: 13906598

Holtz99: Holtz KM, Kantrowitz ER (1999). "The mechanism of the alkaline phosphatase reaction: insights from NMR, crystallography and site-specific mutagenesis." FEBS Lett 462(1-2);7-11. PMID: 10580082

Horiuchi59: Horiuchi T, Horiuchi S, Mizuno D (1959). "A possible negative feedback phenomenon controlling formation of alkaline phosphomonoesterase in Escherichia coli." Nature 183(4674);1529-30. PMID: 13666805

Inouye77: Inouye H, Beckwith J (1977). "Synthesis and processing of an Escherichia coli alkaline phosphatase precursor in vitro." Proc Natl Acad Sci U S A 74(4);1440-4. PMID: 323853

Janeway93: Janeway CM, Xu X, Murphy JE, Chaidaroglou A, Kantrowitz ER (1993). "Magnesium in the active site of Escherichia coli alkaline phosphatase is important for both structural stabilization and catalysis." Biochemistry 1993;32(6);1601-9. PMID: 8431439

Kadokura09: Kadokura H, Beckwith J (2009). "Detecting folding intermediates of a protein as it passes through the bacterial translocation channel." Cell 138(6);1164-73. PMID: 19766568

Kelley73: Kelley PM, Neumann PA, Shriefer K, Cancedda F, Schlesinger MJ, Bradshaw RA (1973). "Amino acid sequence of Escherichia coli alkaline phosphatase. Amino- and carboxyl-terminal sequences and variations between two isozymes." Biochemistry 12(18);3499-503. PMID: 4581334

Kikuchi81: Kikuchi Y, Yoda K, Yamasaki M, Tamura G (1981). "The nucleotide sequence of the promoter and the amino-terminal region of alkaline phosphatase structural gene (phoA) of Escherichia coli." Nucleic Acids Res 1981;9(21);5671-8. PMID: 6273802

Kim91: Kim EE, Wyckoff HW (1991). "Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis." J Mol Biol 1991;218(2);449-64. PMID: 2010919

Le02a: Le Du MH, Lamoure C, Muller BH, Bulgakov OV, Lajeunesse E, Menez A, Boulain JC (2002). "Artificial evolution of an enzyme active site: structural studies of three highly active mutants of Escherichia coli alkaline phosphatase." J Mol Biol 316(4);941-53. PMID: 11884134

Ma95a: Ma L, Tibbitts TT, Kantrowitz ER (1995). "Escherichia coli alkaline phosphatase: X-ray structural studies of a mutant enzyme (His-412-->Asn) at one of the catalytically important zinc binding sites." Protein Sci 4(8);1498-506. PMID: 8520475

Ma96a: Ma L, Kantrowitz ER (1996). "Kinetic and X-ray structural studies of a mutant Escherichia coli alkaline phosphatase (His-412-->Gln) at one of the zinc binding sites." Biochemistry 35(7);2394-402. PMID: 8652582

Makino86: Makino K, Shinagawa H, Amemura M, Nakata A (1986). "Nucleotide sequence of the phoB gene, the positive regulatory gene for the phosphate regulon of Escherichia coli K-12." J Mol Biol 190(1);37-44. PMID: 3537313

Malamy61: Malamy M, Horecker BL (1961). "The localization of alkaline phosphatase in E. coli K12." Biochem Biophys Res Commun 5;104-8. PMID: 13765699

Malamy64: Malamy MH, Horecker BL (1964). "Release of alkaline phosphatase from cells of Escherichia coli upon lysozyme spheroplast formation." Biochemistry 3;1889-93. PMID: 14269305

Malamy64a: Malamy, MH, Horecker, BL "Purification and Crystallization of the Alkaline Phosphatase of Escherichia coli." Biochemistry 3:1893-1897 (1964).

Michaelis83: Michaelis S, Inouye H, Oliver D, Beckwith J (1983). "Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli." J Bacteriol 154(1);366-74. PMID: 6339478

Nakata77: Nakata A, Amemura M, Yamaguchi M, Izutani K (1977). "Factors affecting the formation of alkaline phosphatase isozymes in Escherichia coli K-12." Biken J 20(2);47-55. PMID: 337967

Nakata78: Nakata A, Yamaguchi M, Izutani K, Amemura M (1978). "Escherichia coli mutants deficient in the production of alkaline phosphatase isozymes." J Bacteriol 134(1);287-94. PMID: 348683

Nakata84: Nakata A, Shinagawa H, Shima H (1984). "Alkaline phosphatase isozyme conversion by cell-free extract of Escherichia coli." FEBS Lett 175(2);343-8. PMID: 6383868

Nesmeyanova81: Nesmeyanova MA, Motlokh OB, Kolot MN, Kulaev IS (1981). "Multiple forms of alkaline phosphatase from Escherichia coli cells with repressed and derepressed biosynthesis of the enzyme." J Bacteriol 146(2);453-9. PMID: 7012129

Plocke62: Plocke DJ, Vallee BL (1962). "Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents." Biochemistry 1;1039-43. PMID: 13944069

Plocke62a: Plocke DJ, Levinthal C, Vallee BL (1962). "Alkaline phosphatase of Escherichia coli: a zinc metalloenzyme." Biochemistry 1;373-8. PMID: 14487220

Reid71: Reid TW, Wislon IB (1971). "E.coli Alkaline Phosphatase." The Enzymes 3rd ed. (Boyer PD ed.) 4;373-415.

Schlesinger68: Schlesinger MJ, Andersen L (1968). "Multiple molecular forms of the alkaline phosphatase of Escherichia coli." Ann N Y Acad Sci 151(1);159-70. PMID: 4887360

Schlesinger68a: Schlesinger MJ (1968). "Secretion of alkaline phosphatase subunits by spheroplasts of Escherichia coli." J Bacteriol 96(3);727-33. PMID: 4979102

Schwartz61: Schwartz JH, Lipmann F (1961). "Phosphate incorporation into alkaline phosphatase of E. coli." Proc Natl Acad Sci U S A 47;1996-2005. PMID: 13909705

Sowadski85: Sowadski JM, Handschumacher MD, Murthy HM, Foster BA, Wyckoff HW (1985). "Refined structure of alkaline phosphatase from Escherichia coli at 2.8 A resolution." J Mol Biol 1985;186(2);417-33. PMID: 3910843

Stankiewicz88: Stankiewicz PJ, Gresser MJ (1988). "Inhibition of phosphatase and sulfatase by transition-state analogues." Biochemistry 1988;27(1);206-12. PMID: 3280015

Stec00: Stec B, Holtz KM, Kantrowitz ER (2000). "A revised mechanism for the alkaline phosphatase reaction involving three metal ions." J Mol Biol 299(5);1303-11. PMID: 10873454

Stec98: Stec B, Hehir MJ, Brennan C, Nolte M, Kantrowitz ER (1998). "Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102." J Mol Biol 277(3);647-62. PMID: 9533886

Stigbrand82: Stigbrand T, Millan JL, Fishman WH (1982). "The genetic basis of alkaline phosphatase isozyme expression." Isozymes Curr Top Biol Med Res 6;93-117. PMID: 6762368

Torriani60: Torriani A (1960). "Influence of inorganic phosphate in the formation of phosphatases by Escherichia coli." Biochim Biophys Acta 38;460-9. PMID: 13838951

Torriani68: Torriani A (1968). "Alkaline phosphatase subunits and their dimerization in vivo." J Bacteriol 96(4);1200-7. PMID: 4879556

Torriani90: Torriani A (1990). "From cell membrane to nucleotides: the phosphate regulon in Escherichia coli." Bioessays 12(8);371-6. PMID: 2241934

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Wilson64a: Wilson IB, Dayan J, Cyr K (1964). "Some properties of alkaline phosphatase from Escherichia coli. Transphosphorylation." J Biol Chem 239;4182-5. PMID: 14247666

Yang04a: Yang K, Metcalf WW (2004). "A new activity for an old enzyme: Escherichia coli bacterial alkaline phosphatase is a phosphite-dependent hydrogenase." Proc Natl Acad Sci U S A 101(21);7919-24. PMID: 15148399


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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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