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Antranilat fosforiboziltransferaza
	Antranilat fosforiboziltransferaza homodimer, Mycobacterium tuberculosis
Identifikatori
EC broj	2.4.2.18
CAS broj	9059-35-2
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

Antranilat fosforiboziltransferaza (EC 2.4.2.18, fosforibozil-antranilat pirofosforilaza, PRT, antranilat 5-fosforibozilpirofosfat fosforiboziltransferaza, antranilat fosforibozilpirofosfat fosforiboziltransferaza, fosforibozilantranilat pirofosforilaza, fosforibozilantranilat transferaza, antranilat-PP-riboza-P fosforiboziltransferaza) je enzim sa sistematskim imenom N-(5-fosfo-D-ribozil)-antranilat:difosfat fosfo-alfa-D-riboziltransferaza.^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

N-(5-fosfo-D-ribozil)-antranilat + difosfat

\rightleftharpoons

antranilat + 5-fosfo-alfa-D-riboza 1-difosfat

Kod pojedinih organizama, ovaj enzim je deo multifunkcionalnog proteina zajedno sa jednom ili više komponenti sistema za biosintezu triptofana, cf. EC 4.1.1.48 (indol-3-glicerol-fosfat sintaza), EC 4.1.3.27 (antranilat sintaza), EC 4.2.1.20 (triptofan sintaza) i EC 5.3.1.24 (fosforibozilantranilat izomeraza).

Reference

↑ Creighton, T.E. and Yanofsky, C. (1970). „Chorismate to tryptophan (Escherichia coli) - anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase”. Methods Enzymol. 17A: 365-380.
↑ Hütter, R., Niederberger, P. and DeMoss, J.A. (1986). „Tryptophan synthetic genes in eukaryotic microorganisms”. Annu. Rev. Microbiol. 40: 55-77. PMID 3535653.
↑ Ito, J. and Yanofsky, C. (1969). „Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: Comparative studies on the complex and the subunits”. J. Bacteriol. 97: 734-742. PMID 4886290.
↑ Wegman, J. and DeMoss, J.A. (1965). „The enzymatic conversion of anthranilate to indolylglycerol phosphate in Neurospora crassa”. J. Biol. Chem. 240: 3781-3788. PMID 5842052.

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 Anthranilate+phosphoribosyltransferase

[1] Creighton, T.E. and Yanofsky, C. (1970). „Chorismate to tryptophan (Escherichia coli) - anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase”. Methods Enzymol. 17A: 365-380.

[2] Hütter, R., Niederberger, P. and DeMoss, J.A. (1986). „Tryptophan synthetic genes in eukaryotic microorganisms”. Annu. Rev. Microbiol. 40: 55-77. PMID 3535653.

[3] Ito, J. and Yanofsky, C. (1969). „Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: Comparative studies on the complex and the subunits”. J. Bacteriol. 97: 734-742. PMID 4886290.

[4] Wegman, J. and DeMoss, J.A. (1965). „The enzymatic conversion of anthranilate to indolylglycerol phosphate in Neurospora crassa”. J. Biol. Chem. 240: 3781-3788. PMID 5842052.

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