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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
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Escherichia coli K-12 substr. MG1655 Reaction: 4.2.1.104

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

EC Number: 4.2.1.104

Enzymes and Genes:
cyanase Inferred from experiment : cynS

In Pathway: cyanate degradation

Supersedes EC numbers: 4.3.99.1, 3.5.5.3

Note that this reaction equation differs from the official Enzyme Commission reaction equations for this EC number.

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: cyanase

Enzyme Commission Synonyms: cyanate lyase, cyanate hydrolase, cyanate aminohydrolase, cyanate C-N-lyase, cyanate hydratase

Enzyme Commission Summary:
This enzyme, which is found in bacteria and plants, is used to decompose cyanate, which can be used as the sole source of nitrogen [Kozliak95, Walsh00]. Reaction (1) can be considered as the reverse of 'carbamate = cyanate + H2O', where this is assisted by reaction with bicarbonate and carbon dioxide [Johnson87c], and hence is classified in sub-subclass 4.2.1. Bicarbonate functions as a recycling substrate [Johnson87c].

Citations: [Anderson80, Taussig60, Taussig65, Anderson94a]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:4.2.1.104 , ENZYME:EC:4.2.1.104 , IUBMB-ExplorEnz:EC:4.2.1.104


References

Anderson80: Anderson PM (1980). "Purification and properties of the inducible enzyme cyanase." Biochemistry 19(13);2882-8. PMID: 6994799

Anderson94a: Anderson PM, Korte JJ, Holcomb TA (1994). "Reaction of the N-terminal methionine residues in cyanase with diethylpyrocarbonate." Biochemistry 1994;33(47);14121-5. PMID: 7947823

Johnson87c: Johnson WV, Anderson PM (1987). "Bicarbonate is a recycling substrate for cyanase." J Biol Chem 262(19);9021-5. PMID: 3110153

Kozliak95: Kozliak EI, Fuchs JA, Guilloton MB, Anderson PM (1995). "Role of bicarbonate/CO2 in the inhibition of Escherichia coli growth by cyanate." J Bacteriol 177(11);3213-9. PMID: 7768821

Taussig60: Taussig A (1960). "The synthesis of the induced enzyme, ''cyanase'', in E. coli." Biochim Biophys Acta 44;510-9. PMID: 13775509

Taussig65: Taussig A (1965). "Some properties of the induced enzyme cyanase." Can J Biochem 43(7);1063-9. PMID: 5322950

Walsh00: Walsh MA, Otwinowski Z, Perrakis A, Anderson PM, Joachimiak A (2000). "Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site." Structure 8(5);505-14. PMID: 10801492


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sun Dec 21, 2014, biocyc13.