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Beta-ketoacil-(acil-nosilac-protein) sintaza III
Identifikatori
EC broj	2.3.1.180
CAS broj	1048646-78-1
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

Beta-ketoacil-(acil-nosilac-protein) sintaza III (EC 2.3.1.180, 3-oksoacil:ACP sintaza III, 3-ketoacil-acil nosilac protein sintaza III, KASIII, KAS III, FabH, beta-ketoacil-acil nosilac protein sintaza III, beta-ketoacil-ACP sintaza III, beta-ketoacil (acil nosilac protein) sintaza III, acetil-KoA:malonil-(acil-nosilac-protein) C-aciltransferaza) je enzim sa sistematskim imenom acetil-KoA:malonil-(acil-nosilac protein) C-aciltransferaza.^[1]^[2]^[3]^[4]^[5]^[6]^[7] Ovaj enzim katalizuje sledeću hemijsku reakciju

acetil-KoA + malonil-[acil-nosilac protein]

\rightleftharpoons

acetoacetil-[acil-nosilac protein] + KoA + CO₂

Ovaj enzim učestvuje u sistemu biosinteze disociranih masnih kiselina kod biljki i bakterija.

Reference

↑ Tsay, J.T., Oh, W., Larson, T.J., Jackowski, S. and Rock, C.O. (1992). „Isolation and characterization of the β-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12”. J. Biol. Chem. 267: 6807-6814. PMID 1551888.
↑ Han, L., Lobo, S. and Reynolds, K.A. (1998). „Characterization of β-ketoacyl-acyl carrier protein synthase III from Streptomyces glaucescens and its role in initiation of fatty acid biosynthesis”. J. Bacteriol. 180: 4481-4486. PMID 9721286.
↑ Khandekar, S.S., Gentry, D.R., Van Aller, G.S., Warren, P., Xiang, H., Silverman, C., Doyle, M.L., Chambers, P.A., Konstantinidis, A.K., Brandt, M., Daines, R.A. and Lonsdale, J.T. (2001). „Identification, substrate specificity, and inhibition of the Streptococcus pneumoniae β-ketoacyl-acyl carrier protein synthase III (FabH)”. J. Biol. Chem. 276: 30024-30030. PMID 11375394.
↑ Choi, K.H., Kremer, L., Besra, G.S. and Rock, C.O. (2000). „Identification and substrate specificity of β-ketoacyl (acyl carrier protein) synthase III (mtFabH) from Mycobacterium tuberculosis”. J. Biol. Chem. 275: 28201-28207. PMID 10840036.
↑ Qiu, X., Choudhry, A.E., Janson, C.A., Grooms, M., Daines, R.A., Lonsdale, J.T. and Khandekar, S.S. (2005). „Crystal structure and substrate specificity of the β-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus”. Protein Sci. 14: 2087-2094. PMID 15987898.
↑ Li, Y., Florova, G. and Reynolds, K.A. (2005). „Alteration of the fatty acid profile of Streptomyces coelicolor by replacement of the initiation enzyme 3-ketoacyl acyl carrier protein synthase III (FabH)”. J. Bacteriol. 187: 3795-3799. PMID 15901703.
↑ Cronan, J.E., Jr. and Rock, C.O. (1996). „Biosynthesis of membrane lipids”. u: Neidhardt, F.C.. Escherichia coli and Salmonella: Cellular and Molecular Biology. 1 (2nd izd.). Washington, DC: ASM Press. str. 612-636.

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.

Cronan, J.E., Jr. and Rock, C.O. (1996). „Biosynthesis of membrane lipids”. u: Neidhardt, F.C.. Escherichia coli and Salmonella: Cellular and Molecular Biology. 1 (2nd izd.). Washington, DC: ASM Press. str. 612-636.