Glucosaminate ammonia-lyase

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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.

[edit] References

IUBMB entry for 4.3.1.9
BRENDA references for 4.3.1.9 (Recommended.)
PubMed references for 4.3.1.9
PubMed Central references for 4.3.1.9
Google Scholar references for 4.3.1.9
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Iwamoto R, Imanaga Y, Soda K (Tokyo). "D-glucosaminate dehydratase from Agrobacterium radiobacter Physicochemical and enzymological properties". J. Biochem.: 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: 408–11. PMID 7766176.