The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 2.4.1.11     
Accepted name: glycogen(starch) synthase
Reaction: UDP-α-D-glucose + [(1→4)-α-D-glucosyl]n = UDP + [(1→4)-α-D-glucosyl]n+1
For diagram of glycogen, click here
Other name(s): UDP-glucose—glycogen glucosyltransferase; glycogen (starch) synthetase; UDP-glucose-glycogen glucosyltransferase; UDP-glycogen synthase; UDPG-glycogen synthetase; UDPG-glycogen transglucosylase; uridine diphosphoglucose-glycogen glucosyltransferase; UDP-glucose:glycogen 4-α-D-glucosyltransferase
Systematic name: UDP-α-D-glucose:glycogen 4-α-D-glucosyltransferase (configuration-retaining)
Comments: The accepted name varies according to the source of the enzyme and the nature of its synthetic product (cf. EC 2.4.1.1, phosphorylase). Glycogen synthase from animal tissues is a complex of a catalytic subunit and the protein glycogenin. The enzyme requires glucosylated glycogenin as a primer; this is the reaction product of EC 2.4.1.186 (glycogenin glucosyltransferase). A similar enzyme utilizes ADP-glucose (EC 2.4.1.21, starch synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9014-56-6
References:
1.  Algranati, I.D. and Cabib, E. The synthesis of glycogen in yeast. Biochim. Biophys. Acta 43 (1960) 141–142. [DOI] [PMID: 13682402]
2.  Basu, D.K. and Bachhawat, B.K. Purification of uridine diphosphoglucose-glycogen transglucosylase from sheep brain. Biochim. Biophys. Acta 50 (1961) 123–128. [DOI] [PMID: 13687710]
3.  Leloir, L.F. and Cardini, C.E. UDPG-glycogen transglucosylase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 6, Academic Press, New York, 1962, pp. 317–326.
4.  Leloir, L.F. and Goldemberg, S.H. Synthesis of glycogen from uridine diphosphate glucose in liver. J. Biol. Chem. 235 (1960) 919–923. [PMID: 14415527]
5.  Pitcher, J., Smythe, C. and Cohen, P. Glycogenin is the priming glucosyltransferase required for the initiation of glycogen biogenesis in rabbit skeletal muscle. Eur. J. Biochem. 176 (1988) 391–395. [DOI] [PMID: 2970965]
[EC 2.4.1.11 created 1961]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald