The Enzyme Database

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EC 4.3.1.9     
Accepted name: glucosaminate ammonia-lyase
Reaction: 2-amino-2-deoxy-D-gluconate = 2-dehydro-3-deoxy-D-gluconate + NH3 (overall reaction)
(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)
Glossary: 2-amino-2-deoxy-D-gluconate = glucosaminate
Other name(s): glucosaminic dehydrase; D-glucosaminate dehydratase; D-glucosaminic acid dehydrase; aminodeoxygluconate dehydratase; 2-amino-2-deoxy-D-gluconate hydro-lyase (deaminating); aminodeoxygluconate ammonia-lyase; 2-amino-2-deoxy-D-gluconate ammonia-lyase; D-glucosaminate ammonia-lyase; D-glucosaminate ammonia-lyase (isomerizing; 2-dehydro-3-deoxy-D-gluconate-forming)
Systematic name: 2-amino-2-deoxy-D-gluconate ammonia-lyase (isomerizing; 2-dehydro-3-deoxy-D-gluconate-forming)
Comments: Contains pyridoxal phosphate. 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: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37290-91-8
References:
1.  Imanaga, Y. Metabolism of D-glucosamine. III. Enzymic degradation of D-glucosaminic acid. J. Biochem. (Tokyo) 45 (1958) 647–650.
2.  Merrick, J.M. and Roseman, S. D-Glucosaminic acid dehydrase. Methods Enzymol. 9 (1966) 657–660.
3.  Iwamoto, R., Imanaga, Y. and Soda, K. D-Glucosaminate dehydratase from Agrobacterium radiobacter. Physicochemical and enzymological properties. J. Biochem. (Tokyo) 91 (1982) 283–289. [PMID: 7068563]
4.  Iwamoto, R., Taniki, H., Koishi, J. and Nakura, S. D-Glucosaminate aldolase activity of D-glucosaminate dehydratase from Pseudomonas fluorescens and its requirement for Mn2+ ion. Biosci. Biotechnol. Biochem. 59 (1995) 408–411. [DOI] [PMID: 7766176]
[EC 4.3.1.9 created 1972, (EC 4.3.1.21 created 1965 as EC 4.2.1.26, transferred 2002 to EC 4.3.1.21, incorporated 2004) modified 2004]
 
 


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