Information on EC 4.4.1.24 - (2R)-sulfolactate sulfo-lyase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
4.4.1.24
-
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RECOMMENDED NAME
GeneOntology No.
(2R)-sulfolactate sulfo-lyase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2R)-3-sulfolactate = pyruvate + HSO3-
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(R)-cysteate degradation
-
-
sulfolactate degradation I
-
-
Cysteine and methionine metabolism
-
-
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SYSTEMATIC NAME
IUBMB Comments
(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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strongly inducible enzyme, gene suyAB
SwissProt
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R)-3-sulfolactate
pyruvate + bisulfite
show the reaction diagram
3-sulfolactate
pyruvate + bisulfite
show the reaction diagram
additional information
?
-
activity with 3-sulfopyruvate in vivo by cysteate-grown cells only after membrane permeabilization
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-sulfolactate
pyruvate + bisulfite
show the reaction diagram
Q58Y44
desulfonation step involved in cysteate dissimilation, metabolic pathway in the cell, overview
-
-
?
additional information
?
-
Q58Y44
activity with 3-sulfopyruvate in vivo by cysteate-grown cells only after membrane permeabilization
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
can substitute for Fe2+ at 2mM
Fe2+
required for activity
Mn2+
can substitute for Fe2+ at 2mM
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
70% inhibition at 1 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.016
-
crude extract
0.13
-
crude extract
0.2
-
in the soluble fraction
0.3
purified enzyme
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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
Manually annotated by BRENDA team
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8000
x * 8000, alpha-subunit, + x * 42000, beta-subunit, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 8000, alpha-subunit, + x * 42000, beta-subunit, SDS-PAGE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
after freezing no residual enzyme activity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 1 day, 50% loss of activity
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from cysteate-grown cells by anion exchange chromatography and hydrophobic interaction chromatography, to near homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene suyAB, DNA and amino acid sequence determination and analysis
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Show AA Sequence (126 entries)
Please use the Sequence Search for a specific query.
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LINKS TO OTHER DATABASES (specific for EC-Number 4.4.1.24)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)