| 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 |
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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, glycogen 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 (glycosyl-transferring)]. |
| Links to other databases: |
BRENDA, EXPASY, Gene, 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] |
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| [EC 2.4.1.11 created 1961] |
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