Biology:Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
alpha,alpha-trehalose-phosphate synthase (UDP-forming) | |||||||||
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Identifiers | |||||||||
EC number | 2.4.1.15 | ||||||||
CAS number | 9030-07-3 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, an alpha,alpha-trehalose-phosphate synthase (UDP-forming) (EC 2.4.1.15) is an enzyme that catalyzes the chemical reaction
- UDP-glucose + D-glucose 6-phosphate [math]\displaystyle{ \rightleftharpoons }[/math] UDP + alpha,alpha-trehalose 6-phosphate
Thus, the two substrates of this enzyme are UDP-glucose and D-glucose 6-phosphate, whereas its two products are UDP and alpha,alpha'-trehalose 6-phosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:D-glucose-6-phosphate 1-alpha-D-glucosyltransferase. Other names in common use include UDP-glucose-glucose-phosphate glucosyltransferase, trehalosephosphate-UDP glucosyltransferase, UDP-glucose-glucose-phosphate glucosyltransferase, alpha,alpha-trehalose phosphate synthase (UDP-forming), phosphotrehalose-uridine diphosphate transglucosylase, trehalose 6-phosphate synthase, trehalose 6-phosphate synthetase, trehalose phosphate synthase, trehalose phosphate synthetase, trehalose phosphate-uridine diphosphate glucosyltransferase, trehalose-P synthetase, transglucosylase, and uridine diphosphoglucose phosphate glucosyltransferase. This enzyme participates in starch and sucrose metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1GZ5, 1UQT, and 1UQU.
References
- "The biosynthesis of trehalose phosphate". J. Biol. Chem. 231 (1): 259–75. 1958. PMID 13538966.
- "The biosynthesis of trehalose in the locust fat body". Biochem. J. 78 (3): 531–6. 1961. doi:10.1042/bj0780531. PMID 13690400.
- "Purification and Properties of the Transglucosylase Inhibitor of Mycobacterium Tuberculosis". J. Biol. Chem. 239: 2730–4. 1964. PMID 14216421.
- "The Enzymes of Glycogen and Trehalose Synthesis in Silk Moth Fat Body". J. Biol. Chem. 240: 1500–8. 1965. PMID 14285483.
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