EC |
4.1.1.128 |
Accepted name: |
UDP-N-acetyl-α-D-glucosaminuronate decarboxylase |
Reaction: |
UDP-N-acetyl-α-D-glucosaminuronate = UDP-N-acetyl-α-D-xylosamine + CO2 |
Other name(s): |
UXNAcS; DP-XylNAc synthase |
Systematic name: |
UDP-N-acetyl-α-D-glucosaminuronate carboxy-lyase |
Comments: |
The enzyme has been described from pathogenic Bacillus species, including Bacillus anthracis, Bacillus thuringiensis, and Bacillus cereus. The enzyme requires an NAD cofactor, and the reaction proceeds via a 4-dehydro intermediate, resulting in reduction of NAD+ to NADH (cf. EC 1.1.1.305, UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)). However, NADH is not released from the enzyme and is recycled back to NAD+ at the completion of the reaction cycle. The product is incorporated into an extracellular polysaccharide known as pzX. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Gu, X., Glushka, J., Lee, S.G. and Bar-Peled, M. Biosynthesis of a new UDP-sugar, UDP-2-acetamido-2-deoxyxylose, in the human pathogen Bacillus cereus subspecies cytotoxis NVH 391-98. J. Biol. Chem. 285 (2010) 24825–24833. [DOI] [PMID: 20529859] |
2. |
Li, Z., Hwang, S. and Bar-Peled, M. Discovery of a Unique Extracellular Polysaccharide in Members of the Pathogenic Bacillus That Can Co-form with Spores. J. Biol. Chem. 291 (2016) 19051–19067. [DOI] [PMID: 27402849] |
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[EC 4.1.1.128 created 2024] |
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