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MetaCyc Enzyme: D-mannonate oxidoreductase

Gene: uxuB Accession Numbers: EG20248 (MetaCyc), b4323, ECK4314

Species: Escherichia coli K-12 substr. MG1655

Summary:
D-mannonate oxidoreductase is an enzyme of the D-glucuronate degradation pathway, reducing D-fructuronate to D-mannonate.

The reaction proceeds via a rapid-equilibrium random bi-bi + dead-end EBQ complex mechanism [Portalier72c]. Reports differ on whether [MandrandBerthel77] or not [Portalier72] the enzyme is able to use D-glucuronate as a substrate. Where it was measured, the reaction with D-glucuronate appears to proceed via a different mechanism [MandrandBerthel77].

The enzyme is induced by both glucuronate and fructuronate [Portalier72]; the internal inducer is fructuronate [RobertBaudouy74].

Locations: cytosol

Map Position: [4,550,924 -> 4,552,384]

Molecular Weight of Polypeptide: 53.58 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0014175 , CGSC:13 , DIP:DIP-11109N , EchoBASE:EB4150 , EcoGene:EG20248 , EcoliWiki:b4323 , ModBase:P39160 , OU-Microarray:b4323 , PortEco:uxuB , PR:PRO_000024207 , Pride:P39160 , Protein Model Portal:P39160 , RefSeq:NP_418743 , RegulonDB:EG20248 , SMR:P39160 , String:511145.b4323 , Swiss-Model:P39160 , UniProt:P39160

Relationship Links: InterPro:IN-FAMILY:IPR000669 , InterPro:IN-FAMILY:IPR008927 , InterPro:IN-FAMILY:IPR013118 , InterPro:IN-FAMILY:IPR013131 , InterPro:IN-FAMILY:IPR013328 , InterPro:IN-FAMILY:IPR016040 , InterPro:IN-FAMILY:IPR023027 , Pfam:IN-FAMILY:PF01232 , Pfam:IN-FAMILY:PF08125 , Prints:IN-FAMILY:PR00084 , Prosite:IN-FAMILY:PS00974

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0042840 - D-glucuronate catabolic process Inferred from experiment [Ritzenthaler80]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01]
GO:0019594 - mannitol metabolic process Inferred by computational analysis [GOA01]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0008866 - fructuronate reductase activity Inferred from experiment Inferred by computational analysis [GOA01a, Ritzenthaler80, Portalier72]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016616 - oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred by computational analysis [GOA01]
GO:0050662 - coenzyme binding Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism carbon utilization carbon compounds

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


Enzymatic reaction of: D-mannonate oxidoreductase

Synonyms: fructuronate reductase, D-mannonate:NAD+ 5-oxidoreductase, D-mannonic dehydrogenase

EC Number: 1.1.1.57

D-mannonate + NAD+ <=> D-fructuronate + NADH + 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.

This reaction is reversible. [Portalier72]

Alternative Substrates for NADH: NADPH [Portalier72 ]

Alternative Substrates for D-mannonate: D-altronate [Portalier72 , Hickman60 ]

Alternative Substrates for D-fructuronate: D-tagaturonate [Linster04 , Hickman60 , MandrandBerthel77 , Portalier72 ] , D-glucuronate [MandrandBerthel77 ]

In Pathways: superpathway of hexuronide and hexuronate degradation , superpathway of microbial D-galacturonate and D-glucuronate degradation , superpathway of β-D-glucuronide and D-glucuronate degradation , D-fructuronate degradation

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

Summary:
The optimal pH for fructuronate reduction is 6.3, while the optimal pH for the reverse reaction, oxidation of mannonate, is 8.4. NADPH can substitute for NADH; the Km is 700 µM [Portalier72].

Activators (Unknown Mechanism): Mg2+ [Portalier72] , Ca2+ [Portalier72] , Mn2+ [Portalier72] , Zn2+ [Portalier72]

Inhibitors (Competitive): ATP [MandrandBerthel77] , NAD+ [Portalier72c, MandrandBerthel77]

Inhibitors (Noncompetitive): p-chloromercuribenzoate [Hickman60, Portalier72]

Kinetic Parameters:

Substrate
Km (μM)
Citations
D-fructuronate
1000.0
[Hickman60, BRENDA14]
D-fructuronate
500.0
[Portalier82, BRENDA14]
D-fructuronate
500.0
[Portalier72, BRENDA14]
NADH
30.0
[Portalier72]
D-mannonate
1700.0
[Portalier72d, BRENDA14]
D-mannonate
1800.0
[Portalier72, BRENDA14]
D-mannonate
780.0
[Portalier82, BRENDA14]
D-mannonate
780.0
[Portalier72c, BRENDA14]
NAD+
200.0
[Portalier72]

pH(opt): 6 [BRENDA14, Hickman60], 8.4 [BRENDA14, Portalier82], 6.3 [Portalier72]


Sequence Features

Feature Class Location Citations Comment
Nucleotide-Phosphate-Binding-Region 25 -> 36
[UniProt10a]
UniProt: NAD; Non-Experimental Qualifier: by similarity;

History:
10/20/97 Gene b4323 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG20248; confirmed by SwissProt match.


References

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

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

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Hickman60: Hickman J, Ashwell G (1960). "Uronic acid metabolism in bacteria. II. Purification and properties of D-altronic acid and D-mannonic acid dehydrogenases in Escherichia coli." J Biol Chem 235;1566-70. PMID: 14401695

Linster04: Linster CL, Van Schaftingen E (2004). "A spectrophotometric assay of D-glucuronate based on Escherichia coli uronate isomerase and mannonate dehydrogenase." Protein Expr Purif 37(2);352-60. PMID: 15358357

MandrandBerthel77: Mandrand-Berthelot MA, Lagarde AE (1977). ""Hit-and-run" mechanism for D-glucuronate reduction catalyzed by D-mannonate:NAD oxidoreductase of Escherichia coli." Biochim Biophys Acta 1977;483(1);6-23. PMID: 195622

Portalier72: Portalier RC, Stoeber FR (1972). "[D-mannonate: NAD oxidoreductase from Escherichia coli K12. Purification, properties and specificity]." Eur J Biochem 1972;26(2);290-300. PMID: 4402996

Portalier72c: Portalier RC (1972). "[D-mannonate: NAD-oxidoreductase from Escherichia coli K12. Kinetic studies of the enzymatic mechanism]." Eur J Biochem 1972;30(2);220-33. PMID: 4351435

Portalier72d: Portalier RC, Stoeber FR (1972). "[Colorimetric determinations of aldonate oxidoreductases of Escherichia coli K 12: applications]." Biochim Biophys Acta 289(1);19-27. PMID: 4564054

Portalier82: Portalier R, Stoeber F (1982). "D-Mannonate and D-altronate-NAD dehydrogenases from Escherichia coli." Methods Enzymol 89 Pt D;210-8. PMID: 6755169

Ritzenthaler80: Ritzenthaler P, Mata-Gilsinger M, Stoeber F (1980). "Construction and expression of hybrid plasmids containing Escherichia coli K-12 uxu genes." J Bacteriol 143(3);1116-26. PMID: 6997264

RobertBaudouy74: Robert-Baudouy JM, Portalier RC (1974). "[Studies of mutations in glucuronate catabolism in Escherichia coli K12 (author's transl)]." Mol Gen Genet 131(1);31-46. PMID: 4603847

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Nov 23, 2014, BIOCYC13B.