Mannonate dehydratase

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.

Structural studies

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

References

ASHWELL A, WAHBA AJ, HICKMAN J (1958). "A new pathway of uronic acid metabolism". Biochim. Biophys. Acta 30 (1): 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 (2): 473–85. doi:10.1016/0005-2744(73)90045-4. PMID 4581499.

Carbon-oxygen lyases (EC 4.2) (primarily dehydratases)

4.2.1: Hydro-Lyases	Carbonic anhydrase Fumarase Aconitase Enolase Alpha Enolase 2 Enoyl-CoA hydratase/3-Hydroxyacyl ACP dehydrase Methylglutaconyl-CoA hydratase Tryptophan synthase Cystathionine beta synthase Porphobilinogen synthase 3-Isopropylmalate dehydratase Urocanase Uroporphyrinogen III synthase Nitrile hydratase

4.2.2: Acting on polysaccharides	Hyaluronate lyase

4.2.3: Acting on phosphates	Threonine synthase

4.2.99: Other	Carboxymethyloxysuccinate lyase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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