| EC |
2.4.1.347 |
| Accepted name: |
α,α-trehalose-phosphate synthase (ADP-forming) |
| Reaction: |
ADP-α-D-glucose + D-glucose 6-phosphate = ADP + α,α-trehalose 6-phosphate |
| Other name(s): |
otsA (gene name); ADP-glucose—glucose-phosphate glucosyltransferase |
| Systematic name: |
ADP-α-D-glucose:D-glucose-6-phosphate 1-α-D-glucosyltransferase (configuration-retaining) |
| Comments: |
The enzyme has been reported from the yeast Saccharomyces cerevisiae and from mycobacteria. The enzyme from Mycobacterium tuberculosis can also use UDP-α-D-glucose, but the activity with ADP-α-D-glucose, which is considered the main substrate in vivo, is higher. |
| Links to other databases: |
BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9030-07-3 |
| References: |
| 1. |
Ferreira, J.C., Thevelein, J.M., Hohmann, S., Paschoalin, V.M., Trugo, L.C. and Panek, A.D. Trehalose accumulation in mutants of Saccharomyces cerevisiae deleted in the UDPG-dependent trehalose synthase-phosphatase complex. Biochim. Biophys. Acta 1335 (1997) 40–50. [DOI] [PMID: 9133641] |
| 2. |
Pan, Y.T., Carroll, J.D. and Elbein, A.D. Trehalose-phosphate synthase of Mycobacterium tuberculosis. Cloning, expression and properties of the recombinant enzyme. Eur. J. Biochem. 269 (2002) 6091–6100. [DOI] [PMID: 12473104] |
| 3. |
Asencion Diez, M.D., Demonte, A.M., Syson, K., Arias, D.G., Gorelik, A., Guerrero, S.A., Bornemann, S. and Iglesias, A.A. Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis. Biochim. Biophys. Acta 1850 (2015) 13–21. [DOI] [PMID: 25277548] |
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| [EC 2.4.1.347 created 2017] |
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