EC 126.96.36.199 - Glucosaminate ammonia-lyase
IntEnz Enzyme Nomenclature
2-amino-2-deoxy-D-gluconate hydro-lyase (deaminating)
D-glucosaminic acid dehydrase
acetylenemonocarboxylic acid hydrase
D-glucosaminate ammonia-lyase (isomerizing; 2-dehydro-3-deoxy-D-gluconate-forming)
- (1) 2-amino-2-deoxy-D-gluconate = 2-dehydro-3-deoxy-D-gluconate + NH3
- (1a) 2-amino-2-deoxy-D-gluconate = (2Z,4S,5R)-2-amino-4,5,6-trihydroxyhex-2-enoate + H2O
- (1b) (2Z,4S,5R)-2-amino-4,5,6-trihydroxyhex-2-enoate = (4S,5R)-4,5,6-trihydroxy-2-iminohexanoate (spontaneous)
- (1c) (4S,5R)-4,5,6-trihydroxy-2-iminohexanoate + H2O = 2-dehydro-3-deoxy-D-gluconate + NH3 (spontaneous)
A pyridoxal-phosphate protein. The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes spontaneous hydrolytic deamination to form the final product.
Links to other databases
Metabolism of D-glucosamine. III. Enzymic degradation of D-glucosaminic acid.J. Biochem. (Tokyo) 45: 647-650 (1958).
D-Glucosaminic acid dehydrase.Methods Enzymol. 9: 657-660 (1966).
D-Glucosaminate dehydratase from Agrobacterium radiobacter. Physicochemical and enzymological properties.J. Biochem. (Tokyo) 91: 283-289 (1982). [PMID: 7068563]
D-Glucosaminate aldolase activity of D-glucosaminate dehydratase from Pseudomonas fluorescens and its requirement for Mn2+ ion.Biosci. Biotechnol. Biochem. 59: 408-411 (1995). [PMID: 7766176]
[EC 188.8.131.52 created 1972 (EC 184.108.40.206 created 1965 as EC 220.127.116.11, transferred 2002 to EC 18.104.22.168, incorporated 2004)]