Sucrose synthase
Ribbon diagram of Sucrose Synthase-1 3S27 Structure, isolated from Arabidopsis thaliana.[1]
| sucrose synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.4.1.13 | ||||||||
| CAS number | 9030-05-1 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
| Sucrose synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Sucrose_synth | ||||||||
| Pfam | PF00862 | ||||||||
| InterPro | IPR000368 | ||||||||
| |||||||||
In enzymology, a sucrose synthase (EC 2.4.1.13) is an enzyme that catalyzes the chemical reaction
- NDP-glucose + D-fructose NDP + sucrose
Thus, the two substrates of this enzyme are NDP-glucose and D-fructose, whereas its two products are NDP and sucrose.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is NDP-glucose:D-fructose 2-alpha-D-glucosyltransferase. Other names in common use include UDPglucose-fructose glucosyltransferase, sucrose synthetase, sucrose-UDP glucosyltransferase, sucrose-uridine diphosphate glucosyltransferase, and uridine diphosphoglucose-fructose glucosyltransferase. This enzyme participates in starch and sucrose metabolism.
References
- ↑ Zheng, Yi; Spencer, A.; Zhang, Y.; Garavito, R.M. (24 August 2011). "The Structure of Sucrose Synthase-1 from Arabidopsis thaliana and its Functional Implications". Journal of Biological Chemistry. doi:10.1074/jbc.M111.275974.; rendered with PyMOL
Literature
- Avigad G; Milner Y (1966). "UDP-glucose:fructose transglucosylase from sugar beet roots". Methods Enzymol. 8: 341–345. doi:10.1016/0076-6879(66)08063-7.
- CARDINI CE, LELOIR LF, CHIRIBOGA J (1955). "The biosynthesis of sucrose". J. Biol. Chem. 214 (1): 149–55. PMID 14367373.
- Delmer DP (1972). "The purification and properties of sucrose synthetase from etiolated Phaseolus aureus seedlings". J. Biol. Chem. 247 (12): 3822–8. PMID 4624446.
- Murata T, Sugiyama T, Minamikawa T, Akazawa T (1966). "Enzymic mechanism of starch synthesis in ripening rice grains. 3 Mechanism of the sucrose-starch conversion". Arch. Biochem. Biophys. 113 (1): 34–44. doi:10.1016/0003-9861(66)90153-6. PMID 5941994.
- Yoshinaga F, Mori H, Sakai F, Hayashi T (1998). "An increase in apparent affinity for sucrose of mung bean sucrose synthase is caused by in vitro phosphorylation or directed mutagenesis of Ser11". Plant. Cell. Physiol. 39 (12): 1337–41. PMID 10050318.
- Porchia AC, Curatti L, Salerno GL (1999). "Sucrose metabolism in cyanobacteria: sucrose synthase from Anabaena sp. strain PCC 7119 is remarkably different from the plant enzymes with respect to substrate affinity and amino-terminal sequence". Planta. 210 (1): 34–40. doi:10.1007/s004250050651. PMID 10592030.
- Ross, HA, Davies HV (1992). "Purification and characterization of sucrose synthase from the cotyledons of Vicia fava L". Plant Physiol. 100 (2): 1008–1013. doi:10.1104/pp.100.2.1008.
- Silvius JE; Snyder FW (1979). "Comparative enzymic studies of sucrose metabolism in the taproots and fibrous roots of Beta vulgaris L". Plant Physiol. 64 (6): 1070–1073. doi:10.1104/pp.64.6.1070.
- Tanase K, Yamaki S (2000). "Purification and characterization of two sucrose synthase isoforms from Japanese pear fruit". Plant. Cell. Physiol. 41 (4): 408–14. doi:10.1093/pcp/41.4.408. PMID 10845453.
- T, Pozueta-Romero J; Muñoz, FJ; Saikusa, T; Rodríguez-López, M; Akazawa, T; Pozueta-Romero, J (2003). "Sucrose synthase catalyzes the de novo production of ADPglucose linked to starch biosynthesis in heterotrophic tissues of plants". Plant. Cell. Physiol. 44 (5): 500–9. doi:10.1093/pcp/pcg062. PMID 12773636.
This article is issued from Wikipedia - version of the 8/10/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.