Mannonate dehydratase

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In enzymology, a mannonate dehydratase (EC 4.2.1.8) is an enzyme that catalyzes the chemical reaction

D-mannonate $\rightleftharpoons$ 2-dehydro-3-deoxy-D-gluconate + H₂O

Hence, this enzyme has one substrate, D-mannonate, and two products, 2-dehydro-3-deoxy-D-gluconate and H₂O.

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-mannonate hydro-lyase (2-dehydro-3-deoxy-D-gluconate-forming). Other names in common use include mannonic hydrolase, mannonate hydrolyase, altronic hydro-lyase, altronate hydrolase, D-mannonate hydrolyase, and D-mannonate hydro-lyase. This enzyme participates in pentose and glucuronate interconversions.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1TZ9.

[edit] References

IUBMB entry for 4.2.1.8
BRENDA references for 4.2.1.8 (Recommended.)
PubMed references for 4.2.1.8
PubMed Central references for 4.2.1.8
Google Scholar references for 4.2.1.8
ASHWELL A, WAHBA AJ, HICKMAN J (1958). "A new pathway of uronic acid metabolism". Biochim. Biophys. Acta. 30: 186–7. doi:10.1016/0006-3002(58)90257-9. PMID 13584413.
Robert-Baudouy JM, Stoeber FR (1973). "[Purification and properties of D-mannonate hydrolyase from Escherichia coli K12]". Biochim. Biophys. Acta. 309: 473–85. PMID 4581499.