Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 1.14.13.1

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

EC Number: 1.14.13.1

Enzymes and Genes:
salicylate 1-hydroxylase Inferred from experiment : salA ( Pseudomonas reinekei )

In Pathway: chlorosalicylate degradation

Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .

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: salicylate 1-monooxygenase

Enzyme Commission Synonyms: salicylate hydroxylase, salicylate 1-hydroxylase, salicylate monooxygenase, salicylate hydroxylase (decarboxylating)

Standard Gibbs Free Energy (ΔrG in kcal/mol): -92.624695 Inferred by computational analysis [Latendresse, 2013]

Enzyme Commission Summary:
A flavoprotein (FAD).

Citations: [Nikodem03, Uzuki69, Takemori69, Takemori69a, Yamamoto65]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:1.14.13.1 , ENZYME:EC:1.14.13.1 , IUBMB-ExplorEnz:EC:1.14.13.1


References

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

Nikodem03: Nikodem P, Hecht V, Schlomann M, Pieper DH (2003). "New bacterial pathway for 4- and 5-chlorosalicylate degradation via 4-chlorocatechol and maleylacetate in Pseudomonas sp. strain MT1." J Bacteriol 185(23);6790-800. PMID: 14617643

Takemori69: Takemori S, Yasuda H, Mihara K, Suzuki K, Katagiri M (1969). "Mechanism of the salicylate hydroxylase reaction. II. The enzyme-substrate complex." Biochim Biophys Acta 191(1);58-68. PMID: 4898626

Takemori69a: Takemori S, Yasuda H, Mihara K, Suzuki K, Katagiri M (1969). "Mechanism of the salicylate hydroxylase reaction. 3. Characterization and reactivity of chemically or photochemically reduced enzyme-flavin." Biochim Biophys Acta 191(1);69-76. PMID: 4309912

Uzuki69: Uzuki K, Takemori S, Katagiri M (1969). "Mechanism of the salicylate hydroxylase reaction. IV. Fluorometric analysis of the complex formation." Biochim Biophys Acta 191(1);77-85. PMID: 4390441

Yamamoto65: Yamamoto, S., Katagiri, M., Maeno, H., Hayaishi, O. (1965). "Salicylate hydroxylase, a monooxygenase requiring flavin adenine dinucleotide. I. Purification and general properties." J Biol Chem 240: 3408-13. PMID: 14321380


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 Sat Nov 22, 2014, BIOCYC14B.