5-Metiltioriboza-1-fosfatna izomeraza

5-Metiltioriboza-1-fosfatna izomeraza
Identifikatori
EC broj	5.3.1.23
CAS broj	91608-95-6
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

5-Metiltioriboza-1-fosfatna izomeraza (EC 5.3.1.23, metiltioriboza 1-fosfat izomeraza, 1-PMTR izomeraza, 5-metiltio-5-dezoksi-D-riboza-1-fosfat ketol-izomeraza, S-metil-5-tio-5-dezoksi-D-riboza-1-fosfat ketol-izomeraza, S-metil-5-tio-5-dezoksi-D-riboza-1-fosfat aldoza-ketose-izomeraza, 1-fosfo-5'-S-metiltioriboza izomeraza, S-metil-5-tio-D-riboza-1-fosfat aldoza-ketoza-izomeraza) je enzim sa sistematskim imenom S-metil-5-tio-alfa-D-riboza-1-fosfat aldoza-ketoza-izomeraza.^[1]^[2]^[3] Ovaj enzim katalizuje sledeću hemijsku reakciju

S-metil-5-tio-alfa-D-riboza 1-fosfat

\rightleftharpoons

S-metil-5-tio-D-ribuloza 1-fosfat

Reference uredi

↑ Ghoda, L.Y., Savarese, T.M., Dexter, D.L., Parks, R.E., Jr., Trackman, P.C. and Abeles, R.H. (1984). „Characterization of a defect in the pathway for converting 5′-deoxy-5′-methylthioadenosine to methionine in a subline of a cultured heterogeneous human colon carcinoma”. J. Biol. Chem. 259: 6715-6719. PMID 6725268.
↑ Trackman, P.C. and Abeles, R.H. (1983). „Methionine synthesis from 5′-S-methylthioadenosine. Resolution of enzyme activities and identification of 1-phospho-5-S-methylthioribulose”. J. Biol. Chem. 258: 6717-6720. PMID 6853500.
↑ Furfine, E.S. and Abeles, R.H. (1988). „Intermediates in the conversion of 5′-S-methylthioadenosine to methionine in Klebsiella pneumoniae”. J. Biol. Chem. 263: 9598-9606. PMID 2838472.

Literatura uredi

Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). 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 izd.). Wiley Classics Library. ISBN 0471303097.
Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.

Spoljašnje veze uredi

MeSH S-methyl-5-thioribose-1-phosphate+isomerase

[1] Ghoda, L.Y., Savarese, T.M., Dexter, D.L., Parks, R.E., Jr., Trackman, P.C. and Abeles, R.H. (1984). „Characterization of a defect in the pathway for converting 5′-deoxy-5′-methylthioadenosine to methionine in a subline of a cultured heterogeneous human colon carcinoma”. J. Biol. Chem. 259: 6715-6719. PMID 6725268.

[2] Trackman, P.C. and Abeles, R.H. (1983). „Methionine synthesis from 5′-S-methylthioadenosine. Resolution of enzyme activities and identification of 1-phospho-5-S-methylthioribulose”. J. Biol. Chem. 258: 6717-6720. PMID 6853500.

[3] Furfine, E.S. and Abeles, R.H. (1988). „Intermediates in the conversion of 5′-S-methylthioadenosine to methionine in Klebsiella pneumoniae”. J. Biol. Chem. 263: 9598-9606. PMID 2838472.

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