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IUBMB Comments Requires iron(II). This inducible enzyme participates in cysteate degradation by the bacterium Paracoccus pantotrophus NKNCYSA and in 3-sulfolactate degradation by the bacterium Chromohalobacter salexigens. The enzyme is specific for the (R) isomer of its substrate.
Word Map
4.4.1.24
uv-induced
photolyase
pyrimidone
light-dependent
cyclobutane
photoreceptor
peptide-mass
photoproducts
6-4photoproducts
tripartite
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
(R)-sulfolactate sulfo-lyase, 3-sulfolactate sulfo-lyase, desulfonative sulfolactate sulfo-lyase, More, Suy, SuyAB,
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(R)-sulfolactate sulfo-lyase
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3-sulfolactate sulfo-lyase
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desulfonative sulfolactate sulfo-lyase
additional information
the enzyme belongs to the altronate dehydratase family
desulfonative sulfolactate sulfo-lyase
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desulfonative sulfolactate sulfo-lyase
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SuyAB
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(2R)-3-sulfolactate = pyruvate + hydrogensulfite
(2R)-3-sulfolactate = pyruvate + hydrogensulfite
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(2R)-3-sulfolactate = pyruvate + hydrogensulfite
putative reaction mechanism
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(2R)-3-sulfolactate bisulfite-lyase (pyruvate-forming)
Requires iron(II). This inducible enzyme participates in cysteate degradation by the bacterium Paracoccus pantotrophus NKNCYSA and in 3-sulfolactate degradation by the bacterium Chromohalobacter salexigens. The enzyme is specific for the (R) isomer of its substrate.
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(2R)-3-sulfolactate
pyruvate + bisulfite
3-sulfolactate
pyruvate + bisulfite
additional information
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activity with 3-sulfopyruvate in vivo by cysteate-grown cells only after membrane permeabilization
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(2R)-3-sulfolactate
pyruvate + bisulfite
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(2R)-3-sulfolactate
pyruvate + bisulfite
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(2R)-3-sulfolactate
pyruvate + bisulfite
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3-sulfolactate
pyruvate + bisulfite
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3-sulfolactate
pyruvate + bisulfite
desulfonation step involved in cysteate dissimilation, metabolic pathway in the cell, overview
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3-sulfolactate
pyruvate + bisulfite
desulfonation step involved in cysteate dissimilation, metabolic pathway in the cell, overview
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additional information
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activity with 3-sulfopyruvate in vivo by cysteate-grown cells only after membrane permeabilization
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Co2+
can substitute for Fe2+ at 2mM
Fe2+
required for activity
Mn2+
can substitute for Fe2+ at 2mM
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EDTA
70% inhibition at 1 mM
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additional information
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inducible enzyme activity, activity detected in extract of sulfolactate-grown cells
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additional information
the enzyme is strongly inducible
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0.2
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in the soluble fraction
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strongly inducible enzyme, gene suyAB
SwissProt
brenda
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i.e. 2-amino-3-sulfopropionate, is the sole carbon and energy source of the organism with either nitrate or molecular oxygen as terminal electron acceptor
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8000
x * 8000, alpha-subunit, + x * 42000, beta-subunit, SDS-PAGE
42000
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SDS-PAGE
42000
x * 8000, alpha-subunit, + x * 42000, beta-subunit, SDS-PAGE
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x * 8000, alpha-subunit, + x * 42000, beta-subunit, SDS-PAGE
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after freezing no residual enzyme activity
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4°C, 1 day, 50% loss of activity
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from cysteate-grown cells by anion exchange chromatography and hydrophobic interaction chromatography, to near homogeneity
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gene suyAB, DNA and amino acid sequence determination and analysis
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Rein, U.; Gueta, R.; Denger, K.; Ruff, J.; Hollemeyer, K.; Cook, A.M.
Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA
Microbiology
151
737-747
2005
Paracoccus pantotrophus (Q58Y44)
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Mayer, J.; Huhn, T.; Habeck, M.; Denger, K.; Hollemeyer, K.; Cook, A.M.
2,3-Dihydroxypropane-1-sulfonate degraded by Cupriavidus pinatubonensis JMP134: purification of dihydroxypropanesulfonate 3-dehydrogenase
Microbiology
156
1556-1564
2010
Cupriavidus pinatubonensis
brenda
Denger, K.; Cook, A.M.
Racemase activity effected by two dehydrogenases in sulfolactate degradation by Chromohalobacter salexigens: purification of (S)-sulfolactate dehydrogenase
Microbiology
156
967-974
2010
Chromohalobacter salexigens
brenda
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