EC 2.4.1.347 - α,α-trehalose-phosphate synthase (ADP-forming)

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IntEnz Enzyme Nomenclature
EC 2.4.1.347

Names

Accepted name:
α,α-trehalose-phosphate synthase (ADP-forming)
Other names:
otsA (gene name)
ADP-glucose—glucose-phosphate glucosyltransferase
Systematic name:
ADP-α-D-glucose:D-glucose-6-phosphate 1-α-D-glucosyltransferase (configuration-retaining)

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (16) [show] [UniProt]

References

  1. Ferreira, J. C., Thevelein, J. M., Hohmann, S., Paschoalin, V. M., Trugo, L. C., Panek, A. D.
    Trehalose accumulation in mutants of Saccharomyces cerevisiae deleted in the UDPG-dependent trehalose synthase-phosphatase complex.
    Biochim. Biophys. Acta 1335: 40-50 (1997). [PMID: 9133641]
  2. Pan, Y. T., Carroll, J. D., Elbein, A. D.
    Trehalose-phosphate synthase of Mycobacterium tuberculosis. Cloning, expression and properties of the recombinant enzyme.
    Eur. J. Biochem. 269: 6091-6100 (2002). [PMID: 12473104]
  3. Asencion Diez, M. D., Demonte, A. M., Syson, K., Arias, D. G., Gorelik, A., Guerrero, S. A., Bornemann, S., Iglesias, A. A.
    Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis.
    Biochim. Biophys. Acta 1850: 13-21 (2015). [PMID: 25277548]

[EC 2.4.1.347 created 2017]