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3-dehidrohinatna sintaza
Identifikatori
EC broj	4.2.3.4
CAS broj	37211-77-1
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

3-dehidrohinatna sintaza (EC 4.2.3.4, 5-dehidrohinat sintaza, 5-dehidrohinatno kiselinska sintetaza, dehidrohinatna sintaza, 3-dehidrohinatna sintetaza, 3-dezoksi-arabino-heptulozonat-7-fosfat fosfat-lijaza (ciklizacija), 3-dezoksi-arabino-heptulonat-7-fosfat fosfat-lijaza (ciklizacija), 3-dezoksi-arabino-heptulonat-7-fosfat fosfat-lijaza (ciklizacija, formira 3-dehidrohinat)) je enzim sa sistematskim imenom 3-dezoksi-D-arabino-hept-2-ulosonat-7-fosfat fosfat-lijaza (ciklizacija, formira 3-dehidrohinat).^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

3-dezoksi-D-arabino-hept-2-ulosonat 7-fosfat

\rightleftharpoons

3-dehidrohinat + fosfat

Za dejstvo ovog enzima je neophodan jon Co²⁺ i vezani NAD⁺.

Reference

↑ Rotenberg, S.L. and Sprinson, D.B. (1970). „Mechanism and stereochemistry of 5-dehydroquinate synthetase”. Proc. Natl. Acad. Sci. USA 67: 1669-1672. PMID 5275368.
↑ Srinivasan, P.R., Rothschild, J. and Sprinson, D.B. (1963). „The enzymic conversion of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate to 5-dehydroquinate”. J. Biol. Chem. 238: 3176-3182. PMID 14085358.
↑ Bender, S.L., Mehdi, S. and Knowles, J.R. (1989). „Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis”. Biochemistry 28: 7555-7560. PMID 2514789.
↑ Carpenter, E.P., Hawkins, A.R., Frost, J.W. and Brown, K.A. (1998). „Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis”. Nature 394: 299-302. PMID 9685163.

Literatura

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.

Vanjske veze

MeSH 3-dehydroquinate+synthase

[1] Rotenberg, S.L. and Sprinson, D.B. (1970). „Mechanism and stereochemistry of 5-dehydroquinate synthetase”. Proc. Natl. Acad. Sci. USA 67: 1669-1672. PMID 5275368.

[2] Srinivasan, P.R., Rothschild, J. and Sprinson, D.B. (1963). „The enzymic conversion of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate to 5-dehydroquinate”. J. Biol. Chem. 238: 3176-3182. PMID 14085358.

[3] Bender, S.L., Mehdi, S. and Knowles, J.R. (1989). „Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis”. Biochemistry 28: 7555-7560. PMID 2514789.

[4] Carpenter, E.P., Hawkins, A.R., Frost, J.W. and Brown, K.A. (1998). „Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis”. Nature 394: 299-302. PMID 9685163.

[1]

[2]

[3]

[4]

3-Dehidrohinatna sintaza

Reference

Literatura

Vanjske veze