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Antocijanidin 3-O-glukoziltransferaza
Antocijanidin 3-O-glukoziltransferaza
Identifikatori
EC broj	2.4.1.115
CAS broj	65607-32-1
Baze podataka
IntEnz	IntEnz pregled
BRENDA	BRENDA pristup
ExPASy	NiceZyme pregled
KEGG	KEGG pristup
MetaCyc	metabolički put
PRIAM	profil
Strukture PBP	RCSB PDB PDBe PDBj PDBsum
PMC
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PMC	članci
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NCBI	proteini

Antocijanidin 3-O-glukoziltransferaza (EC 2.4.1.115, uridin difosfoglukoza-antocijanidinska 3-O-glukoziltransferaza, UDP-glukoza:antocijanidin/flavonol 3-O-glukoziltransferaza, UDP-glukoza:cijanidin-3-O-glukoziltransferaza, UDP-glukoza:antocijanidin 3-O-D-glukoziltransferaza, 3-GT) je enzim sa sistematskim imenom UDP-D-glukoza:antocijanidin 3-O-beta-D-glukoziltransferaza.^[1]^[2]^[3] Ovaj enzim katalizuje sledeću hemijsku reakciju

UDP-D-glukoza + antocijanidin

\rightleftharpoons

UDP + antocijanidin-3-O-beta-D-glukozid

Antocijanidinska jedinjenja cijanidin, delfinidin, peonidin i u manjoj meri pelargonidin mobu da budu supstrati.

Reference

^ Kamsteeg, J., van Brederode, J. and van Nigtevecht, G. (1978). „Identification and properties of UDP-glucose: cyanidin-3-O-glucosyltransferase isolated from petals of the red campion (Silene dioica)”. Biochem. Genet. 16: 1045—1058. PMID 751640.
^ Ford, C.M., Boss, P.K. and Høj, P.B. (1998). „Cloning and characterization of Vitis vinifera UDP-glucose:flavonoid 3-O-glucosyltransferase, a homologue of the enzyme encoded by the maize Bronze-1 locus that may primarily serve to glucosylate anthocyanidins in vivo”. J. Biol. Chem. 273: 9224—9233. PMID 9535914.
^ Nakajima, J., Tanaka, Y., Yamazaki, M. and Saito, K. (2001). „Reaction mechanism from leucoanthocyanidin to anthocyanidin 3-glucoside, a key reaction for coloring in anthocyanin biosynthesis”. J. Biol. Chem. 276: 25797—25803. PMID 11316805.

Literatura

Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036.
Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0.
Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097.

Spoljašnje veze

Anthocyanidin+3-O-glucosyltransferase на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Kamsteeg, J., van Brederode, J. and van Nigtevecht, G. (1978). „Identification and properties of UDP-glucose: cyanidin-3-O-glucosyltransferase isolated from petals of the red campion (Silene dioica)”. Biochem. Genet. 16: 1045—1058. PMID 751640.

[2] Ford, C.M., Boss, P.K. and Høj, P.B. (1998). „Cloning and characterization of Vitis vinifera UDP-glucose:flavonoid 3-O-glucosyltransferase, a homologue of the enzyme encoded by the maize Bronze-1 locus that may primarily serve to glucosylate anthocyanidins in vivo”. J. Biol. Chem. 273: 9224—9233. PMID 9535914.

[3] Nakajima, J., Tanaka, Y., Yamazaki, M. and Saito, K. (2001). „Reaction mechanism from leucoanthocyanidin to anthocyanidin 3-glucoside, a key reaction for coloring in anthocyanin biosynthesis”. J. Biol. Chem. 276: 25797—25803. PMID 11316805.

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