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discounted EARLY registration ends Dec 31, 2014
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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.
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discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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MetaCyc Enzyme: 3-sulfolactate sulfo-lyase

Species: Paracoccus pantotrophus NKNCYSA

Subunit composition of 3-sulfolactate sulfo-lyase = [SuyA][SuyB]
         3-sulfolactate sulfo-lyase small subunit = SuyA (summary available)
         3-sulfolactate sulfo-lyase large subunit = SuyB (summary available)

Summary:
The subunit coefficients in this enzyme complex from Paracoccus pantotrophus NKNCYSA have not been reported.

The nitrite-reducing strain Paracoccus pantotrophus NKNCYSA is able to utilize (RS)-3-sulfolactate (racemic sulfolactate) and L-cysteate, presumably via a membrane transport system. A pathway for L-cysteate degradation has been proposed in this organism that involves sulfolactate as an intermediate and a substrate for this desulfonating enzyme.

Enzyme activity was present in cells grown with L-cysteate or (RS)-3-sulfolactate, but not in cells grown with acetate, taurine, isethionate, or sulfoacetate, indicating an inducible enzyme [Rein05]. The 3-sulfolactate sulfo-lyase enzyme is a heterodimer, composed of a 42 kDa and an 8 kDa subunits. Both subunits were purified to homogeneity, and the purified protein catalyzed the sulfolactate sulfo-lyase reaction [Rein05].

The enantiomeric preference of the enzyme from Paracoccus pantotrophus NKNCYSA has not been established, although an enantiomeric specificity was inferred, along with an inferred racemization step in the pathway [Rein05]. Desulfonation is a key step in bacterial utilization of its carbon and sulfur moieties (as described in the summary for pathway sulfolactate degradation I).

Hypothetical, contiguous suyAB-like genes were found in several different genomes of bacteria, archaea and environmental samples grown with (RS)-3-sulfolactate [Rein05].

Gene-Reaction Schematic: ?

Credits:
Created 23-Sep-2010 by Fulcher CA , SRI International


Enzymatic reaction of: 3-sulfolactate sulfo-lyase

EC Number: 4.4.1.24

(2R)-3-sulfolactate <=> pyruvate + bisulfite

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

The reaction is favored in the direction shown.

In Pathways: (R)-cysteate degradation

Summary:
The assay used for this enzyme was based the disappearance of (RS)-3-sulfolactate (racemic sulfolactate) with stoichiometric formation of pyruvate and bisulfite (sulfite). Experiments using crude extracts suggested a divalent cation requirement of Fe2+, Mn2+ or Co2+ [Rein05].


Subunit of 3-sulfolactate sulfo-lyase: 3-sulfolactate sulfo-lyase small subunit

Synonyms: SuyA

Gene: suyA Accession Number: G-12195 (MetaCyc)

Molecular Weight: 7.328 kD (from nucleotide sequence)

Molecular Weight: 8.0 kD (experimental) [Rein05]

Unification Links: UniProt:Q58Y44

Summary:
The subunit apparent molecular mass was determined by SDS-PAGE [Rein05].


Subunit of 3-sulfolactate sulfo-lyase: 3-sulfolactate sulfo-lyase large subunit

Synonyms: SuyB

Gene: suyB Accession Number: G-12194 (MetaCyc)

Molecular Weight: 42.452 kD (from nucleotide sequence)

Molecular Weight: 42.0 kD (experimental) [Rein05]

Unification Links: UniProt:Q58Y43

Relationship Links: InterPro:IN-FAMILY:IPR007392 , Pfam:IN-FAMILY:PF04295

Summary:
The subunit apparent molecular mass was determined by SDS-PAGE [Rein05].


References

Rein05: Rein U, Gueta R, Denger K, Ruff J, Hollemeyer K, Cook AM (2005). "Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA." Microbiology 151(Pt 3);737-47. PMID: 15758220


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 Dec 20, 2014, biocyc11.