Cistein sintaza

Cistein sintaza
Identifikatori
EC broj 2.5.1.47
CAS broj 37290-89-4
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

Cistein sintaza (EC 2.5.1.47, O-acetil-L-serin sulfhidrilaza, O-acetil-L-serin sulfohidrolaza, O-acetilserin (tiol)-lijaza, O-acetilserin (tiol)-lijaza A, O-acetilserin sulfhidrilaza, O3-acetil-L-serin acetat-lijaza (dodaje vodonik-sulfid), acetilserin sulfhidrilaza, cistein sintetaza, S-sulfocistein sintaza, 3-O-acetil-L-serin:vodonik-sulfid 2-amino-2-karboksietiltransferaza) je enzim sa sistematskim imenom O3-acetil-L-serin:vodonik-sulfid 2-amino-2-karboksietiltransferaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju

O3-acetil-L-serin + vodonik sulfid ⇌ {\displaystyle \rightleftharpoons } L-cistein + acetat

Ovaj enzim je piridoksal-fosfatni protein. Pojedini alkilni tioli, cijanidi, pirazoli i neka druga heterociklična jedinjenja mogu da deluju kao akceptori.

Reference

  1. ↑ Becker, M.A., Kredich, N.M. and Tomkins, G.M. (1969). „The purification and characterization of O-acetylserine sulfhydrylase-A from Salmonella typhimurium”. J. Biol. Chem. 244: 2418-2427. PMID 4891157. 
  2. ↑ Hara, S., Payne, M.A., Schnackerz, K.D. and Cook, P.F. (1990). „A rapid purification procedure and computer-assisted sulfide ion selective electrode assay for O-acetylserine sulfhydrylase from Salmonella typhimurium”. Protein Expr. Purif. 1: 70-76. PMID 2152186. 
  3. ↑ Ikegami, F., Kaneko, M., Lambein, F., Kuo, Y.-H. and Murakoshi, I. (1987). „Difference between uracilylalanine synthases and cysteine synthases in Pisum sativum”. Phytochemistry 26: 2699-2704. 
  4. ↑ Murakoshi, I., Kaneko, M., Koide, C. and Ikegami, F. (1986). „Enzymatic-synthesis of the neuroexcitatory amino-acid quisqualic by cysteine synthase”. Phytochemistry 25: 2759-2763. 
  5. ↑ Tai, C.H., Burkhard, P., Gani, D., Jenn, T., Johnson, C. and Cook, P.F. (2001). „Characterization of the allosteric anion-binding site of O-acetylserine sulfhydrylase”. Biochemistry 40: 7446-7452. PMID 11412097. 
  6. ↑ Bettati, S., Benci, S., Campanini, B., Raboni, S., Chirico, G., Beretta, S., Schnackerz, K.D., Hazlett, T.L., Gratton, E. and Mozzarelli, A. (2000). „Role of pyridoxal 5′-phosphate in the structural stabilization of O-acetylserine sulfhydrylase”. J. Biol. Chem. 275: 40244-40251. PMID 10995767. 

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. 

Spoljašnje veze

  • MeSH Cysteine+synthase
  • p
  • r
  • u
TemeTipovi
EC1 Oksidoreduktaze/spisak  • EC2 Transferaze/spisak  • EC3 Hidrolaze/spisak  • EC4 Lijaze/spisak  • EC5 Izomeraze/spisak  • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6