EC 4.3.1.9 - Glucosaminate ammonia-lyase

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IntEnz Enzyme Nomenclature
EC 4.3.1.9

Names

Accepted name:
glucosaminate ammonia-lyase
Other names:
2-amino-2-deoxy-D-gluconate ammonia-lyase
2-amino-2-deoxy-D-gluconate hydro-lyase (deaminating)
D-glucosaminate dehydratase
D-glucosaminic acid dehydrase
aminodeoxygluconate ammonia-lyase
aminodeoxygluconate dehydratase
glucosaminic dehydrase
acetylenemonocarboxylic acid hydrase
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)

Reactions

Cofactor

Comments:

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047930
CAS Registry Number: 37290-91-8
UniProtKB/Swiss-Prot:

References

  1. Imanaga, Y.
    Metabolism of D-glucosamine. III. Enzymic degradation of D-glucosaminic acid.
    J. Biochem. (Tokyo) 45: 647-650 (1958).
  2. Merrick, J.M. and Roseman, S.
    D-Glucosaminic acid dehydrase.
    Methods Enzymol. 9: 657-660 (1966).
  3. Iwamoto, R., Imanaga, Y. and Soda, K.
    D-Glucosaminate dehydratase from Agrobacterium radiobacter. Physicochemical and enzymological properties.
    J. Biochem. (Tokyo) 91: 283-289 (1982). [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: 408-411 (1995). [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)]