EC number:2.4.1.347

Enzyme

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EC Tree
     2. Transferases
        2.4 Glycosyltransferases
            2.4.1 Hexosyltransferases
ID:2.4.1.347
Description:Alpha,alpha-trehalose-phosphate synthase (ADP-forming).
Alternative Name: ADP-glucose--glucose-phosphate glucosyltransferase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.4.1.347
BRENDA Enzyme Link: BRENDA 2.4.1.347
KEGG Enzyme Link: KEGG2.4.1.347
BioCyc Enzyme Link: BioCyc 2.4.1.347
ExPASy Enzyme Link: ExPASy2.4.1.347
EC2PDB Enzyme Link: EC2PDB 2.4.1.347
ExplorEnz Enzyme Link: ExplorEnz 2.4.1.347
PRIAM enzyme-specific profiles Link: PRIAM 2.4.1.347
IntEnz Enzyme Link: IntEnz 2.4.1.347
MEDLINE Enzyme Link: MEDLINE 2.4.1.347

EC number:2.4.1.347

MSA:

2.4.1.347;
Phylogenetic Tree:

2.4.1.347;
Uniprot:
M-CSA:
RHEA:53880 ADP-alpha-D-glucose + D-glucose 6-phosphate = ADP + alpha,alpha-trehalose 6-phosphate + H(+)
RULE(radius=1) [*:1]-[O;H0;+0:2]-[CH;+0:3](-[*:4])-[*:5].[*:6]-[OH;+0:7]>>[*:4]-[CH;+0:3](-[*:5])-[O;H0;+0:7]-[*:6].[*:1]-[OH;+0:2]
Reaction
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References

TitleAuthorsDatePubMed ID
Trehalose-phosphate synthase of Mycobacterium tuberculosis. Cloning, expression and properties of the recombinant enzyme.Pan YT, Carroll JD, Elbein AD2002 Dec12473104
Trehalose accumulation in mutants of Saccharomyces cerevisiae deleted in the UDPG-dependent trehalose synthase-phosphatase complex.Ferreira JC, Thevelein JM, Hohmann S, Paschoalin VM, Trugo LC, Panek AD1997 Apr 179133641
Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis.Asención Diez MD, Demonte AM, Syson K, Arias DG, Gorelik A, Guerrero SA, Bornemann S, Iglesias AA2015 Jan25277548