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: 1.14.14.5

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

EC Number: 1.14.14.5

Enzymes and Genes:
alkanesulfonate monooxygenase, FMNH2-dependent Inferred from experiment : ssuD ( Escherichia coli K-12 substr. MG1655 )

In Pathway: two-component alkanesulfonate monooxygenase

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.

Instance reactions:
1-butanesulfonate + FMNH2 + oxygen → butanal + sulfite + FMN + H2O + 2 H+ (1.14.14.5)

isethionate + FMNH2 + oxygen → glycolaldehyde + sulfite + FMN + H2O + 2 H+ (1.14.14.5)

3-(N-morpholino)propanesulfonate + FMNH2 + oxygen → 3-(N-morpholino)propanal + sulfite + FMN + H2O + 2 H+ (1.14.14.5)

Enzyme Commission Primary Name: alkanesulfonate monooxygenase

Enzyme Commission Synonyms: SsuD, sulfate starvation-induced protein 6, alkanesulfonate,reduced-FMN:oxygen oxidoreductase

Standard Gibbs Free Energy (ΔrG in kcal/mol): -153.37541 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
The enzyme from Escherichia coli catalyses the desulfonation of a wide range of aliphatic sulfonates (unsubstituted C1- to C14-sulfonates as well as substituted C2-sulfonates). Does not desulfonate taurine (2-aminoethanesulfonate) or aromatic sulfonates. Does not use FMN as a bound cofactor. Instead, it uses reduced FMN (i.e., FMNH2) as a substrate. FMNH2 is provided by SsuE, the associated FMN reductase (EC 1.5.1.38).

Citations: [Eichhorn99]

Gene-Reaction Schematic: ?

Instance reactions of [an alkanesulfonate + FMNH2 + oxygen → an aldehyde + sulfite + FMN + H2O + 2 H+] (1.14.14.5):
i1: 1-butanesulfonate + FMNH2 + oxygen → butanal + sulfite + FMN + H2O + 2 H+ (1.14.14.5)

i2: isethionate + FMNH2 + oxygen → glycolaldehyde + sulfite + FMN + H2O + 2 H+ (1.14.14.5)

i3: 3-(N-morpholino)propanesulfonate + FMNH2 + oxygen → 3-(N-morpholino)propanal + sulfite + FMN + H2O + 2 H+ (1.14.14.5)

Unification Links: KEGG:R07210

Relationship Links: BRENDA:EC:1.14.14.5 , ENZYME:EC:1.14.14.5 , IUBMB-ExplorEnz:EC:1.14.14.5

Credits:
Revised 05-Aug-2009 by Caspi R , SRI International


References

Eichhorn99: Eichhorn E, van der Ploeg JR, Leisinger T (1999). "Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli." J Biol Chem 1999;274(38);26639-46. PMID: 10480865

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


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 Thu Nov 27, 2014, BIOCYC14A.