PROFILPELAJAR.COM

Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

Dihidrofolat reduktaza
Dihidrofolat reduktaza
Identifikatori
EC broj	1.5.1.3
CAS broj	2594015
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
Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

Dihidrofolat reduktaza (EC 1.5.1.3, tetrahidrofolatna dehidrogenaza, DHFR, pteridinska reduktaza:dihidrofolat reduktaza, dihidrofolatna reduktaza:timidilat sintaza, timidilatna sintetaza-dihidrofolat reduktaza, folna kiselina reduktaza, folna reduktaza, dihidrofolna kiselina reduktaza, dihidrofolna reduktaza, 7,8-dihidrofolat reduktaza, NADPH-dihidrofolat reduktaza) je enzim sa sistematskim imenom 5,6,7,8-tetrahidrofolat:NADP⁺ oksidoreduktaza.^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

5,6,7,8-tetrahidrofolat + NADP⁺

\rightleftharpoons

7,8-dihidrofolat + NADPH + H⁺

Ovaj enzim iz životinaj i nekih mikroorganizama takođe u manjoj meri redukuje folat do 5,6,7,8-tetrahidrofolata.

Reference

^ Blakley, R.L. & MacDougall, B.M. (1961). „Dihydrofolic reductase from Streptococcus faecalis R”. J. Biol. Chem. 236: 1163—1163.
^ Bolin, J.T., Filman, D.J., Matthews, D.A. and Kraut, J. (1982). „Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate”. J. Biol. Chem. 257: 13650—13662. PMID 6815178.
^ Kaufman, B.T. & Gardiner, R.C. (1966). „Studies on dihydrofolic reductase. I. Purification and properties of dihydrofolic reductase from chicken liver”. J. Biol. Chem. 241: 1319—1328. PMID 4379915.
^ Young, I.G. & Gibson, F. (1969). „Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli”. Biochim. Biophys. Acta. 177: 401—411. PMID 4306838.

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

Dihydrofolate+reductase на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Blakley, R.L. & MacDougall, B.M. (1961). „Dihydrofolic reductase from Streptococcus faecalis R”. J. Biol. Chem. 236: 1163—1163.

[2] Bolin, J.T., Filman, D.J., Matthews, D.A. and Kraut, J. (1982). „Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate”. J. Biol. Chem. 257: 13650—13662. PMID 6815178.

[3] Kaufman, B.T. & Gardiner, R.C. (1966). „Studies on dihydrofolic reductase. I. Purification and properties of dihydrofolic reductase from chicken liver”. J. Biol. Chem. 241: 1319—1328. PMID 4379915.

[4] Young, I.G. & Gibson, F. (1969). „Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli”. Biochim. Biophys. Acta. 177: 401—411. PMID 4306838.

[1]

[2]

[3]

[4]