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1,5-anhidro-D-fruktoza reduktaza (formira 1,5-anhidro-D-manitol)
1,5-anhidro-D-fruktoza reduktaza (formira 1,5-anhidro-D-manitol)
Identifikatori
EC broj	1.1.1.292
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
PubMed	članci
NCBI	proteini

1,5-anhidro-D-fruktoza reduktaza (formira 1,5-anhidro-D-manitol) (EC 1.1.1.292, 1,5-anhidro-D-fruktozna reduktaza, AFR) je enzim sa sistematskim imenom 1,5-anhidro-D-manitol:NADP⁺ oksidoreduktaza.^[1]^[2] Ovaj enzim katalizuje sledeću hemijsku reakciju

1,5-anhidro-D-manitol + NADP⁺

\rightleftharpoons

1,5-anhidro-D-fruktoza + NADPH + H⁺

Ovaj enzim je prisutan u delu Rhizobium vrsta i pripada familiji GFO/IDH/MocA proteina. On se razlikuje od hepatičke 1,5-anhidro-D-fruktozne reduktaze, koja formira 1,5-anhidro-D-glucitol kao produkt (cf. EC 1.1.1.263). Kod Sinorhizobium morelense, produkt reakcije, 1,5-anhidro-D-manitol, može da bude dalje metabolisan do D-manoze. Ovaj enzim takođe redukuje 1,5-anhidro-D-eritro-hekso-2,3-diulozu i 2-ketoaldoze, kao što je D-glukozon (D-arabino-heksoz-2-uloza) i 6-dezoksi-D-glukozon. On ne redukuje druge aldoze i ketose, niti nešećerne aldehide i ketone.

Reference

^ Kühn, A., Yu, S. and Giffhorn, F. (2006). „Catabolism of 1,5-anhydro-D-fructose in Sinorhizobium morelense S-30.7.5: discovery, characterization, and overexpression of a new 1,5-anhydro-D-fructose reductase and its application in sugar analysis and rare sugar synthesis”. Appl. Environ. Microbiol. 72: 1248—1257. PMID 16461673.
^ Dambe, T.R., Kühn, A.M., Brossette, T., Giffhorn, F. and Scheidig, A.J. (2006). „Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 Å resolution: construction of a NADH-accepting mutant and its application in rare sugar synthesis”. Biochemistry. 45: 10030—10042. PMID 16906761.

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.
William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.

Spoljašnje veze

1,5-anhydro-D-fructose+reductase+(1,5-anhydro-D-mannitol-forming) на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Kühn, A., Yu, S. and Giffhorn, F. (2006). „Catabolism of 1,5-anhydro-D-fructose in Sinorhizobium morelense S-30.7.5: discovery, characterization, and overexpression of a new 1,5-anhydro-D-fructose reductase and its application in sugar analysis and rare sugar synthesis”. Appl. Environ. Microbiol. 72: 1248—1257. PMID 16461673.

[2] Dambe, T.R., Kühn, A.M., Brossette, T., Giffhorn, F. and Scheidig, A.J. (2006). „Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 Å resolution: construction of a NADH-accepting mutant and its application in rare sugar synthesis”. Biochemistry. 45: 10030—10042. PMID 16906761.

[1]

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