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MetaCyc Reaction: 2.5.1.47

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 2.5.1.47

Enzymes and Genes:
cysteine synthase B Inferred from experiment : cysM ( Escherichia coli K-12 substr. MG1655 )
O-acetylserine sulfhydrylase A Inferred from experiment : cysK ( Escherichia coli K-12 substr. MG1655 )
O-ureido-L-serine synthase Inferred from experiment : dcsD ( Streptomyces lavendulae lavendulae )
cysteine synthase Inferred from experiment ( Astragalus bisulcatus )
O-acetylserine (thiol) lyase Inferred from experiment : oasC ( Arabidopsis thaliana col )
O-acetylserine (thiol) lyase Inferred from experiment : oasB ( Arabidopsis thaliana col )
O-acetylserine (thiol) lyase Inferred from experiment : oasA1 ( Arabidopsis thaliana col )

In Pathway: cysteine biosynthesis I

Supersedes EC number: 4.2.99.8

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: cysteine synthase

Enzyme Commission Synonyms: O-acetyl-L-serine sulfhydrylase, O-acetyl-L-serine sulfohydrolase, O-acetylserine (thiol)-lyase, O-acetylserine (thiol)-lyase A, O-acetylserine sulfhydrylase, O3-acetyl-L-serine acetate-lyase (adding hydrogen-sulfide), acetylserine sulfhydrylase, cysteine synθse, S-sulfocysteine synthase, 3-O-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase, O3-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase

Standard Gibbs Free Energy (ΔrG in kcal/mol): -11.374123 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
A pyridoxal-phosphate protein. Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. Not identical with EC 2.5.1.51, β-pyrazolylalanine synthase, EC 2.5.1.52, L-mimosine synthase and EC 2.5.1.53, uracilylalanine synthase.

Citations: [Becker69, Hara90, Tai01, Bettati00, Ikegami87, Murakoshi86]

Gene-Reaction Schematic: ?

Unification Links: KEGG:R00897 , Rhea:14829

Relationship Links: BRENDA:EC:2.5.1.47 , ENZYME:EC:2.5.1.47 , IUBMB-ExplorEnz:EC:2.5.1.47 , UniProt:RELATED-TO:O05393 , UniProt:RELATED-TO:O32978 , UniProt:RELATED-TO:O34476 , UniProt:RELATED-TO:O45679 , UniProt:RELATED-TO:O67507 , UniProt:RELATED-TO:O81154 , UniProt:RELATED-TO:O81155 , UniProt:RELATED-TO:O81523 , UniProt:RELATED-TO:P0A1E3 , UniProt:RELATED-TO:P0A534 , UniProt:RELATED-TO:P0ABK5 , UniProt:RELATED-TO:P16703 , UniProt:RELATED-TO:P29848 , UniProt:RELATED-TO:P31300 , UniProt:RELATED-TO:P32260 , UniProt:RELATED-TO:P37887 , UniProt:RELATED-TO:P38076 , UniProt:RELATED-TO:P45040 , UniProt:RELATED-TO:P47998 , UniProt:RELATED-TO:P47999 , UniProt:RELATED-TO:P53206 , UniProt:RELATED-TO:P56067 , UniProt:RELATED-TO:P63873 , UniProt:RELATED-TO:P71128 , UniProt:RELATED-TO:P80608 , UniProt:RELATED-TO:P87131 , UniProt:RELATED-TO:Q7M1J2 , UniProt:RELATED-TO:Q93244 , UniProt:RELATED-TO:Q9CHF0 , UniProt:RELATED-TO:Q9CI26 , UniProt:RELATED-TO:Q9JQL6 , UniProt:RELATED-TO:Q9RAS8 , UniProt:RELATED-TO:Q9RW80 , UniProt:RELATED-TO:Q9S2H1 , UniProt:RELATED-TO:Q9S6Z7 , UniProt:RELATED-TO:Q9S757 , UniProt:RELATED-TO:Q9SMY4 , UniProt:RELATED-TO:Q9UWP0 , UniProt:RELATED-TO:Q9V1Q3 , UniProt:RELATED-TO:Q9WZD3 , UniProt:RELATED-TO:Q9XDU7 , UniProt:RELATED-TO:Q9ZMW6 , UniProt:RELATED-TO:Q00834 , UniProt:RELATED-TO:Q43153 , UniProt:RELATED-TO:Q43317 , UniProt:RELATED-TO:Q43725 , UniProt:RELATED-TO:Q43726 , UniProt:RELATED-TO:Q59447 , UniProt:RELATED-TO:Q59529

Credits:
Revised 10-Oct-2011 by Caspi R , SRI International


References

Becker69: Becker MA, Kredich NM, Tomkins GM (1969). "The purification and characterization of O-acetylserine sulfhydrylase-A from Salmonella typhimurium." J Biol Chem 244(9);2418-27. PMID: 4891157

Bettati00: Bettati S, Benci S, Campanini B, Raboni S, Chirico G, Beretta S, Schnackerz KD, Hazlett TL, Gratton E, Mozzarelli A (2000). "Role of pyridoxal 5'-phosphate in the structural stabilization of O-acetylserine sulfhydrylase." J Biol Chem 275(51);40244-51. PMID: 10995767

Hara90: Hara S, Payne MA, Schnackerz KD, Cook PF (1990). "A rapid purification procedure and computer-assisted sulfide ion selective electrode assay for O-acetylserine sulfhydrylase from Salmonella typhimurium." Protein Expr Purif 1(1);70-6. PMID: 2152186

Ikegami87: Ikegami F, Kaneko M, Lambein F, Kuo Y-H, Murakoshi I (1987). "Difference between uracilylalanine synthases and cysteine synthases in Pisum sativum." Phytochemistry 26 2699-2704.

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Murakoshi86: Murakoshi I, Kaneko M, Koide C, Ikegami F (1986). "Enzymatic-synthesis of the neuroexcitatory amino-acid quisqualic by cysteine synthase." Phytochemistry 25 2759-2763.

Tai01: Tai CH, Burkhard P, Gani D, Jenn T, Johnson C, Cook PF (2001). "Characterization of the allosteric anion-binding site of O-acetylserine sulfhydrylase." Biochemistry 40(25);7446-52. PMID: 11412097


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Fri Nov 28, 2014, biocyc14.