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词条 Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
释义

  1. Structural studies

  2. References

{{enzyme
| Name = alpha,alpha-trehalose-phosphate synthase (UDP-forming)
| EC_number = 2.4.1.15
| CAS_number = 9030-07-3
| IUBMB_EC_number = 2/4/1/15
| GO_code = 0003825
| image =
| width =
| caption =
}}

In enzymology, an alpha,alpha-trehalose-phosphate synthase (UDP-forming) ({{EC number|2.4.1.15}}) is an enzyme that catalyzes the chemical reaction

UDP-glucose + D-glucose 6-phosphate 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 {{PDB link|1GZ5}}, {{PDB link|1UQT}}, and {{PDB link|1UQU}}.

References

  • {{cite journal |vauthors=CABIB E, LELOIR LF | date = 1958 | title = The biosynthesis of trehalose phosphate | journal = J. Biol. Chem. | volume = 231 | pages = 259–75 | pmid = 13538966 | issue = 1 }}
  • {{cite journal |vauthors=CANDY DJ, KILBY BA | date = 1961 | title = The biosynthesis of trehalose in the locust fat body | journal = Biochem. J. | volume = 78 | pages = 531–6 | pmid = 13690400 | pmc = 1205371 }}
  • {{cite journal |vauthors=LORNITZO FA, GOLDMAN DS | date = 1964 | title = PURIFICATION AND PROPERTIES OF THE TRANSGLUCOSYLASE INHIBITOR OF MYCOBACTERIUM TUBERCULOSIS | journal = J. Biol. Chem. | volume = 239 | pages = 2730–4 | pmid = 14216421 }}
  • {{cite journal |vauthors=MURPHY TA, WYATT GR | date = 1965 | title = THE ENZYMES OF GLYCOGEN AND TREHALOSE SYNTHESIS IN SILK MOTH FAT BODY | journal = J. Biol. Chem. | volume = 240 | pages = 1500–8 | pmid = 14285483 }}
{{Glycosyltransferases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{2.4-enzyme-stub}}

2 : EC 2.4.1|Enzymes of known structure

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