| EC |
3.6.1.45 |
| Accepted name: |
UDP-sugar diphosphatase |
| Reaction: |
UDP-sugar + H2O = UMP + α-D-aldose 1-phosphate |
| Other name(s): |
nucleosidediphosphate-sugar pyrophosphatase; nucleosidediphosphate-sugar diphosphatase; UDP-sugar hydrolase; UDP-sugar pyrophosphatase |
| Systematic name: |
UDP-sugar sugarphosphohydrolase |
| Comments: |
A divalent cation is required for activity. UDP-sugar is the best substrate, although other nucleoside-sugar diphosphates are used as substrates with similar Km values but much lower maximum velocities. Thus, this enzyme has a specificity distinct from that of ADP-sugar diphosphatase (EC 3.6.1.21). Some but not all enzymes of this class also appear to have 5′-nucleotidase (see EC 3.1.3.5) activity. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 55354-38-6 |
| References: |
| 1. |
Garrett, A.R., Johnson, L.A., Beacham, I.R. Isolation, molecular characterization and expression of the ushB gene of Salmonella typhimurium which encodes a membrane bound UDP-sugar hydrolase. Mol. Microbiol. 3 (1989) 177–186. [DOI] [PMID: 2548058] |
| 2. |
Glaser, L., Melo, A., Paul, R. Uridine diphosphate sugar hydrolase. Purification of enzyme and protein inhibitor. J. Biol. Chem. 242 (1987) 1944–1954. [PMID: 5337593] |
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| [EC 3.6.1.45 created 1999] |
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