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Escherichia coli K-12 substr. MG1655 Enzyme: adenylosuccinate synthetase



Gene: purA Accession Numbers: EG10790 (EcoCyc), b4177, ECK4173

Synonyms: adeK

Regulation Summary Diagram: ?

Subunit composition of adenylosuccinate synthetase = [PurA]2

Summary:
Adenylosuccinate synthetase catalyzes the first committed step toward the de novo synthesis of AMP.

The alarmone ppGpp is a regulator of adenylosuccinate synthetase [Pao81, Hou99]. The cyclic nucleotide guanosine 5'-diphosphate 2':3'-cyclic monophosphate binds more tightly to the active site than ppGpp [Hou99].

Extensive kinetic studies of wild-type and mutant enzymes have defined the substrate binding sites and residues involved in catalysis. This work is reviewed in [Honzatko99]. The Asp333 residue appears to be the determinant for GTP specificity [Kang94a].

Intersubunit complementation experiments suggested that the enzyme contains two shared active sites at the dimer interface. The Kd for dimer dissociation is 1 µM, and the presence of IMP stabilizes the dimeric form [Kang96, Wang97d]. The interaction of IMP with the enzyme drives the conformational transition of the active site [Hou02].

Crystal structures of the enzyme have been determined [Poland93, Silva95, Poland96b, Poland96, Poland96a, Poland97, Choe99, Hou99, Hou02, Iancu06], and a catalytic mechanism has been proposed based on these studies.

purA is essential for growth on glycerol minimal medium [Joyce06].

Deletion of purA or purB was shown to result in a decrease in acid resistance, apparently due to the effects of decreased ATP biosynthesis on processes that require ATP for survival under acidic conditions [Sun11].

Review: [Honzatko99]

Gene Citations: [Meng90]

Locations: cytosol, membrane

Map Position: [4,402,710 -> 4,404,008] (94.89 centisomes)
Length: 1299 bp / 432 aa

Molecular Weight of Polypeptide: 47.345 kD (from nucleotide sequence), 48 kD (experimental) [Bass87a ]

Molecular Weight of Multimer: 141 kD (experimental) [Bass87a]

Unification Links: ASAP:ABE-0013672 , CGSC:345 , DIP:DIP-36219N , EchoBASE:EB0783 , EcoGene:EG10790 , EcoliWiki:b4177 , Mint:MINT-1286548 , OU-Microarray:b4177 , PortEco:purA , PR:PRO_000023637 , Pride:P0A7D4 , Protein Model Portal:P0A7D4 , RefSeq:NP_418598 , RegulonDB:EG10790 , SMR:P0A7D4 , String:511145.b4177 , UniProt:P0A7D4

Relationship Links: InterPro:IN-FAMILY:IPR001114 , InterPro:IN-FAMILY:IPR018220 , InterPro:IN-FAMILY:IPR027417 , Panther:IN-FAMILY:PTHR11846 , PDB:Structure:1ADE , PDB:Structure:1ADI , PDB:Structure:1CG0 , PDB:Structure:1CG1 , PDB:Structure:1CG3 , PDB:Structure:1CG4 , PDB:Structure:1CH8 , PDB:Structure:1CIB , PDB:Structure:1GIM , PDB:Structure:1GIN , PDB:Structure:1HON , PDB:Structure:1HOO , PDB:Structure:1HOP , PDB:Structure:1JUY , PDB:Structure:1KJX , PDB:Structure:1KKB , PDB:Structure:1KKF , PDB:Structure:1KSZ , PDB:Structure:1NHT , PDB:Structure:1QF4 , PDB:Structure:1QF5 , PDB:Structure:1SON , PDB:Structure:1SOO , PDB:Structure:2GCQ , Pfam:IN-FAMILY:PF00709 , Prosite:IN-FAMILY:PS00513 , Prosite:IN-FAMILY:PS01266 , Smart:IN-FAMILY:SM00788

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006164 - purine nucleotide biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a, Kang97, Burton71, Joyce06]
GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0015949 - nucleobase-containing small molecule interconversion Inferred from experiment [Bass87a]
GO:0046086 - adenosine biosynthetic process Inferred from experiment [Kang97]
GO:0044208 - 'de novo' AMP biosynthetic process Inferred by computational analysis [UniProtGOA12]
Molecular Function: GO:0004019 - adenylosuccinate synthase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Bass87a, Iancu06]
GO:0005515 - protein binding Inferred from experiment [Zheng11]
GO:0042803 - protein homodimerization activity Inferred from experiment [Bass87a]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0000287 - magnesium ion binding Inferred by computational analysis [GOA06]
GO:0005525 - GTP binding Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0016874 - ligase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05, Lasserre06]
GO:0016020 - membrane Inferred from experiment [Lasserre06]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]

MultiFun Terms: metabolism biosynthesis of building blocks nucleotides purine biosynthesis
metabolism central intermediary metabolism nucleotide and nucleoside conversions

Essentiality data for purA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 0.4% glucose No 37 Aerobic 7.2 0.27 No [Patrick07, Comment 3]
M9 medium with 1% glycerol No 37 Aerobic 7.2 0.35 No [Joyce06]
MOPS medium with 0.4% glucose No 37 Aerobic 7.2 0.22 No [Baba06, Comment 2]
No [Feist07, Comment 4]

Credits:
Curated 11-Jan-2007 by Keseler I , SRI International
Last-Curated ? 20-Dec-2011 by Fulcher C , SRI International


Enzymatic reaction of: adenylosuccinate synthetase

Synonyms: IMP-aspartate ligase, IMP:L-aspartate ligase (GDP-forming), adenylosuccinate synthase, AMPSase

EC Number: 6.3.4.4

L-aspartate + IMP + GTP <=> adenylo-succinate + GDP + phosphate + 2 H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Alternative Substrates for IMP: dIMP [Iancu06 ]

In Pathways: superpathway of histidine, purine, and pyrimidine biosynthesis , superpathway of purine nucleotides de novo biosynthesis II , superpathway of adenosine nucleotides de novo biosynthesis II , adenosine ribonucleotides de novo biosynthesis

Summary:
Early kinetic and enzyme inhibition studies were done with enzyme purified from E. coli B, e.g. [Wyngaarden63, Rudolph69, Stayton79]. Nuclotides such as GDP, GMP, AMP, and dGMP act as competitive inhibitors with respect to GTP, but non-competitive inhibition with IMP and aspartate. In contrast, adenylosuccinate was a competitive inhibitor with respect to IMP.

Inhibition by ppGpp and ppGp is noncompetitive with respect to GTP and competitive with respect to IMP [Pao81].

Cofactors or Prosthetic Groups: Mg2+ [Kang95]

Inhibitors (Competitive): ppGpp [Pao81] , ppGp [Pao81]

Inhibitors (Unknown Mechanism): Zn2+ [Kang95]

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
IMP
20.0
[Honzatko99a, BRENDA14]
IMP
21.0
[Kang94, BRENDA14]
IMP
27.8
[Wang95, BRENDA14]
IMP
47.0
[Stayton83, BRENDA14]
IMP
54.0
[Bass87a, BRENDA14]
IMP
59.6
[Poland96, BRENDA14]
IMP
66.0
[Gorrell02, BRENDA14]
IMP
70.0
[Wang98c, BRENDA14]
IMP
24.0, 24.3
[Dong91, BRENDA14]
IMP
28.0
1.0
[Iancu06, BRENDA14]
GTP
22.0
[Kang94, BRENDA14]
GTP
38.0
[Bass87a, BRENDA14]
GTP
53.5
[Wang97c, BRENDA14]
GTP
190.0
[Gorrell02, BRENDA14]
GTP
22.1
[Dong91]
GTP
26.0
0.96
[Iancu06, BRENDA14]
GTP
1.4
[Honzatko99a, BRENDA14]
GTP
11.0
0.096, 1.59, 2.94
[Wang98c, BRENDA14]
L-aspartate
10.0
[Honzatko99a, BRENDA14]
L-aspartate
230.0
[Gorrell02, BRENDA14]
L-aspartate
191.0
[Dong91]

pH(opt): 7.7 [BRENDA14, Honzatko99], 7.8 [BRENDA14, Wang98c], 7.7 [Wang97c]


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Wolfe88a, Link97, UniProt11a]
UniProt: Removed.
Chain 2 -> 432
[UniProt09]
UniProt: Adenylosuccinate synthetase;
Mutagenesis-Variant 13
[UniProt10a]
Alternate sequence: G → V; UniProt: Significant reduction in activity;
Nucleotide-Phosphate-Binding-Region 13 -> 19
[UniProt10a]
UniProt: GTP;
Metal-Binding-Site 14
[UniProt10a]
UniProt: Magnesium;
Active-Site 14
[UniProt10a]
UniProt: Proton acceptor;
Protein-Segment 14 -> 17
[UniProt10a]
UniProt: IMP binding; Sequence Annotation Type: region of interest;
Mutagenesis-Variant 16
[UniProt10a]
Alternate sequence: G → V; UniProt: Significant reduction in activity;
Mutagenesis-Variant 17
[UniProt10a]
Alternate sequence: K → Q; UniProt: Reduces catalytic efficiency by 50%;
Mutagenesis-Variant 18
[UniProt10a]
Alternate sequence: G → V; UniProt: Significant reduction in activity;
Mutagenesis-Variant 19
[UniProt10a]
Alternate sequence: K → R; UniProt: Significant reduction in activity;
Mutagenesis-Variant 20
[UniProt10a]
Alternate sequence: I → T; UniProt: Significant reduction in activity;
Protein-Segment 39 -> 42
[UniProt10a]
UniProt: IMP binding; Sequence Annotation Type: region of interest;
Metal-Binding-Site 41
[UniProt10a]
UniProt: Magnesium; via carbonyl oxygen;
Nucleotide-Phosphate-Binding-Region 41 -> 43
[UniProt10a]
UniProt: GTP;
Active-Site 42
[UniProt10a]
UniProt: Proton donor;
Amino-Acid-Sites-That-Bind 130
[UniProt10a]
UniProt: IMP;
Mutagenesis-Variant 141
[UniProt10a]
Alternate sequence: K → I; UniProt: Total loss of activity;
Mutagenesis-Variant 144
[UniProt10a]
Alternate sequence: R → L; UniProt: Does not reduce catalytic efficiency;
Amino-Acid-Sites-That-Bind 144
[UniProt10a]
UniProt: IMP; shared with dimeric partner;
Mutagenesis-Variant 148
[Dong91, UniProt11a]
Alternate sequence: R → L; UniProt: Reduced activity.
Amino-Acid-Sites-That-Bind 225
[UniProt10a]
UniProt: IMP;
Amino-Acid-Sites-That-Bind 240
[UniProt10a]
UniProt: IMP;
Protein-Segment 300 -> 306
[UniProt10a]
UniProt: Substrate binding; Sequence Annotation Type: region of interest;
Mutagenesis-Variant 304
[UniProt10a]
Alternate sequence: R → L; UniProt: Reduces catalytic efficiency by 87%;
Amino-Acid-Sites-That-Bind 304
[UniProt10a]
UniProt: IMP;
Amino-Acid-Sites-That-Bind 306
[UniProt10a]
UniProt: GTP;
Nucleotide-Phosphate-Binding-Region 332 -> 334
[UniProt10a]
UniProt: GTP;
Nucleotide-Phosphate-Binding-Region 415 -> 417
[UniProt10a]
UniProt: GTP;
Sequence-Conflict 417
[Wolfe88a, UniProt10a]
Alternate sequence: G → D; UniProt: (in Ref. 1; AAA24446);


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b4177 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10790; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bass87a: Bass MB, Fromm HJ, Stayton MM (1987). "Overproduction, purification, and characterization of adenylosuccinate synthetase from Escherichia coli." Arch Biochem Biophys 1987;256(1);335-42. PMID: 3038024

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Burton71: Burton K (1971). "The limitation of glycolysis in adenine-deficient Escherichia coli." Biochem J 123(4);585-90. PMID: 4942450

Choe99: Choe JY, Poland BW, Fromm HJ, Honzatko RB (1999). "Mechanistic implications from crystalline complexes of wild-type and mutant adenylosuccinate synthetases from Escherichia coli." Biochemistry 38(21);6953-61. PMID: 10346917

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

Dong90: Dong Q, Fromm HJ (1990). "Chemical modification of adenylosuccinate synthetase from Escherichia coli by pyridoxal 5'-phosphate. Identification of an active site lysyl residue." J Biol Chem 265(11);6235-40. PMID: 2108156

Dong91: Dong Q, Liu F, Myers AM, Fromm HJ (1991). "Evidence for an arginine residue at the substrate binding site of Escherichia coli adenylosuccinate synthetase as studied by chemical modification and site-directed mutagenesis." J Biol Chem 1991;266(19);12228-33. PMID: 2061308

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

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."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Gorrell02: Gorrell A, Wang W, Underbakke E, Hou Z, Honzatko RB, Fromm HJ (2002). "Determinants of L-aspartate and IMP recognition in Escherichia coli adenylosuccinate synthetase." J Biol Chem 277(11);8817-21. PMID: 11781326

Honzatko99: Honzatko RB, Fromm HJ (1999). "Structure-function studies of adenylosuccinate synthetase from Escherichia coli." Arch Biochem Biophys 370(1);1-8. PMID: 10496970

Honzatko99a: Honzatko RB, Stayton MM, Fromm HJ (1999). "Adenylosuccinate synthetase: recent developments." Adv Enzymol Relat Areas Mol Biol 73;57-102, ix-x. PMID: 10218106

Hou02: Hou Z, Wang W, Fromm HJ, Honzatko RB (2002). "IMP Alone Organizes the Active Site of Adenylosuccinate Synthetase from Escherichia coli." J Biol Chem 277(8);5970-6. PMID: 11741996

Hou99: Hou Z, Cashel M, Fromm HJ, Honzatko RB (1999). "Effectors of the stringent response target the active site of Escherichia coli adenylosuccinate synthetase." J Biol Chem 274(25);17505-10. PMID: 10364182

Iancu06: Iancu CV, Zhou Y, Borza T, Fromm HJ, Honzatko RB (2006). "Cavitation as a mechanism of substrate discrimination by adenylosuccinate synthetases." Biochemistry 45(38);11703-11. PMID: 16981730

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kang94: Kang C, Fromm HJ (1994). "Characterization of the putative GTP-binding site residues of Escherichia coli adenylosuccinate synthetase by site-directed mutagenesis." Arch Biochem Biophys 310(2);475-80. PMID: 8179335

Kang94a: Kang C, Sun N, Honzatko RB, Fromm HJ (1994). "Replacement of Asp333 with Asn by site-directed mutagenesis changes the substrate specificity of Escherichia coli adenylosuccinate synthetase from guanosine 5'-triphosphate to xanthosine 5'-triphosphate." J Biol Chem 269(39);24046-9. PMID: 7929056

Kang95: Kang C, Fromm HJ (1995). "Identification of an essential second metal ion in the reaction mechanism of Escherichia coli adenylosuccinate synthetase." J Biol Chem 270(26);15539-44. PMID: 7797548

Kang96: Kang C, Kim S, Fromm HJ (1996). "Subunit complementation of Escherichia coli adenylosuccinate synthetase." J Biol Chem 271(47);29722-8. PMID: 8939906

Kang97: Kang C, Sun N, Poland BW, Gorrell A, Honzatko RB, Fromm HJ (1997). "Residues essential for catalysis and stability of the active site of Escherichia coli adenylosuccinate synthetase as revealed by directed mutation and kinetics." J Biol Chem 272(18);11881-5. PMID: 9115248

Khil02: Khil PP, Camerini-Otero RD (2002). "Over 1000 genes are involved in the DNA damage response of Escherichia coli." Mol Microbiol 44(1);89-105. PMID: 11967071

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Link97: Link AJ, Robison K, Church GM (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18(8);1259-313. PMID: 9298646

Liu92: Liu F, Dong Q, Fromm HJ (1992). "Site-directed mutagenesis of the phosphate-binding consensus sequence in Escherichia coli adenylosuccinate synthetase." J Biol Chem 267(4);2388-92. PMID: 1733940

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Meng90: Meng LM, Kilstrup M, Nygaard P (1990). "Autoregulation of PurR repressor synthesis and involvement of purR in the regulation of purB, purC, purL, purMN and guaBA expression in Escherichia coli." Eur J Biochem 1990;187(2);373-9. PMID: 2404765

Pao81: Pao CC, Dyess BT (1981). "Effect of unusual guanosine nucleotides on the activities of some Escherichia coli cellular enzymes." Biochim Biophys Acta 677(3-4);358-62. PMID: 6117328

Patrick07: Patrick WM, Quandt EM, Swartzlander DB, Matsumura I (2007). "Multicopy suppression underpins metabolic evolvability." Mol Biol Evol 24(12);2716-22. PMID: 17884825

Poland93: Poland BW, Silva MM, Serra MA, Cho Y, Kim KH, Harris EM, Honzatko RB (1993). "Crystal structure of adenylosuccinate synthetase from Escherichia coli. Evidence for convergent evolution of GTP-binding domains." J Biol Chem 268(34);25334-42. PMID: 8244965

Poland96: Poland BW, Lee SF, Subramanian MV, Siehl DL, Anderson RJ, Fromm HJ, Honzatko RB (1996). "Refined crystal structure of adenylosuccinate synthetase from Escherichia coli complexed with hydantocidin 5'-phosphate, GDP, HPO4(2-), Mg2+, and hadacidin." Biochemistry 35(49);15753-9. PMID: 8961938

Poland96a: Poland BW, Fromm HJ, Honzatko RB (1996). "Crystal structures of adenylosuccinate synthetase from Escherichia coli complexed with GDP, IMP hadacidin, NO3-, and Mg2+." J Mol Biol 264(5);1013-27. PMID: 9000627

Poland96b: Poland BW, Hou Z, Bruns C, Fromm HJ, Honzatko RB (1996). "Refined crystal structures of guanine nucleotide complexes of adenylosuccinate synthetase from Escherichia coli." J Biol Chem 271(26);15407-13. PMID: 8663109

Poland97: Poland BW, Bruns C, Fromm HJ, Honzatko RB (1997). "Entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coli." J Biol Chem 272(24);15200-5. PMID: 9182542

Rudolph69: Rudolph FB, Fromm HJ (1969). "Initial rate studies of adenylosuccinate synthetase with product and competitive inhibitors." J Biol Chem 244(14);3832-9. PMID: 4896485

Silva95: Silva MM, Poland BW, Hoffman CR, Fromm HJ, Honzatko RB (1995). "Refined crystal structures of unligated adenylosuccinate synthetase from Escherichia coli." J Mol Biol 254(3);431-46. PMID: 7490761

Stayton79: Stayton MM, Fromm HJ (1979). "Guanosine 5'-diphosphate-3'-diphosphate inhibition of adenylosuccinate synthetase." J Biol Chem 1979;254(8);2579-81. PMID: 372184

Stayton83: Stayton MM, Rudolph FB, Fromm HJ (1983). "Regulation, genetics, and properties of adenylosuccinate synthetase: a review." Curr Top Cell Regul 22;103-41. PMID: 6347525

Sun11: Sun Y, Fukamachi T, Saito H, Kobayashi H (2011). "ATP requirement for acidic resistance in Escherichia coli." J Bacteriol 193(12);3072-7. PMID: 21478347

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.

UniProt11a: 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."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Wang95: Wang W, Poland BW, Honzatko RB, Fromm HJ (1995). "Identification of arginine residues in the putative L-aspartate binding site of Escherichia coli adenylosuccinate synthetase." J Biol Chem 270(22);13160-3. PMID: 7768911

Wang97c: Wang W, Hou Z, Honzatko RB, Fromm HJ (1997). "Relationship of conserved residues in the IMP binding site to substrate recognition and catalysis in Escherichia coli adenylosuccinate synthetase." J Biol Chem 272(27);16911-6. PMID: 9202000

Wang97d: Wang W, Gorrell A, Honzatko RB, Fromm HJ (1997). "A study of Escherichia coli adenylosuccinate synthetase association states and the interface residues of the homodimer." J Biol Chem 272(11);7078-84. PMID: 9054400

Wang98c: Wang W, Gorrell A, Hou Z, Honzatko RB, Fromm HJ (1998). "Ambiguities in mapping the active site of a conformationally dynamic enzyme by directed mutation. Role of dynamics in structure-function correlations in Escherichia coli adenylosuccinate synthetase." J Biol Chem 273(26);16000-4. PMID: 9632649

Wolfe88a: Wolfe SA, Smith JM (1988). "Nucleotide sequence and analysis of the purA gene encoding adenylosuccinate synthetase of Escherichia coli K12." J Biol Chem 1988;263(35);19147-53. PMID: 3058695

Wyngaarden63: Wyngaarden JB, Greenland RA (1963). "The inhibition of succinoadenylate kinosynthetase of Escherichia coli by adenosine and guanosine 5'-monophosphates." J Biol Chem 238:1054-1057. PMID: 14002128

Zheng11: Zheng C, Yang L, Hoopmann MR, Eng JK, Tang X, Weisbrod CR, Bruce JE (2011). "Cross-linking measurements of in vivo protein complex topologies." Mol Cell Proteomics 10(10);M110.006841. PMID: 21697552

Other References Related to Gene Regulation

Cho11: Cho BK, Federowicz SA, Embree M, Park YS, Kim D, Palsson BO (2011). "The PurR regulon in Escherichia coli K-12 MG1655." Nucleic Acids Res 39(15);6456-64. PMID: 21572102

He94: He B, Zalkin H (1994). "Regulation of Escherichia coli purA by purine repressor, one component of a dual control mechanism." J Bacteriol 176(4);1009-13. PMID: 8106311

Hommais04: Hommais F, Krin E, Coppee JY, Lacroix C, Yeramian E, Danchin A, Bertin P (2004). "GadE (YhiE): a novel activator involved in the response to acid environment in Escherichia coli." Microbiology 150(Pt 1);61-72. PMID: 14702398

Schneiders04: Schneiders T, Barbosa TM, McMurry LM, Levy SB (2004). "The Escherichia coli transcriptional regulator MarA directly represses transcription of purA and hdeA." J Biol Chem 279(10);9037-42. PMID: 14701822


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, BIOCYC13B.