Glucosaminate ammonia-lyase

glucosaminate ammonia-lyase
Identifiers
EC number	4.3.1.9
CAS number	37290-91-8
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, a glucosaminate ammonia-lyase (EC 4.3.1.9) is an enzyme that catalyzes the chemical reaction

D-glucosaminate $\rightleftharpoons$ 2-dehydro-3-deoxy-D-gluconate + NH₃

Hence, this enzyme has one substrate, D-glucosaminate, and two products, 2-dehydro-3-deoxy-D-gluconate and NH₃.

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is D-glucosaminate ammonia-lyase (isomerizing 2-dehydro-3-deoxy-D-gluconate-forming). Other names in common use include 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, and D-glucosaminate ammonia-lyase. This enzyme participates in pentose phosphate pathway. It employs one cofactor, pyridoxal phosphate.

References

• Imanaga Y (1958). "Metabolism of D-glucosamine. III. Enzymic degradation of D-glucosaminic acid". J. Biochem. (Tokyo) 45: 647–650.
• Merrick JM and Roseman S (1966). "D-Glucosaminic acid dehydrase". Carbohydrate Metabolism. Methods in Enzymology 9. pp. 657–660. doi:10.1016/0076-6879(66)09133-X. ISBN 978-0-12-181809-8.
• Iwamoto R, Imanaga Y, Soda K (Jan 1982). "D-glucosaminate dehydratase from Agrobacterium radiobacter Physicochemical and enzymological properties". J. Biochem. (Tokyo) 91 (1): 283–9. PMID 7068563.
• Iwamoto R, Taniki H, Koishi J, Nakura S (1995). "D-glucosaminate aldolase activity of D-glucosaminate dehydratase from Pseudomonas fluorescens and its requirement for Mn2+ ion". Biosci. Biotechnol. Biochem. 59 (3): 408–11. doi:10.1271/bbb.59.408. PMID 7766176.