Information on EC 3.1.3.71 - 2-phosphosulfolactate phosphatase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

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EC NUMBER
COMMENTARY hide
3.1.3.71
-
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RECOMMENDED NAME
GeneOntology No.
2-phosphosulfolactate phosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2R)-2-phospho-3-sulfolactate + H2O = (2R)-3-sulfolactate + phosphate
show the reaction diagram
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoric ester hydrolysis
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
coenzyme M biosynthesis I
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-
coenzyme M biosynthesis
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Methane metabolism
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Microbial metabolism in diverse environments
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-
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SYSTEMATIC NAME
IUBMB Comments
(R)-2-phospho-3-sulfolactate phosphohydrolase
Requires Mg2+. The enzyme from Methanococcus jannaschii acts on both stereoisoimers of the substrate and also hydrolyses a number of phosphate monoesters of (S)-2-hydroxycarboxylic acids, including 2-phosphomalate, 2-phospholactate and 2-phosphoglycolate. This enzyme can also hydrolyse phosphate monoesters of (R)-2-hydroxycarboxylic acids such as (S)-2-phospho-3-sulfolactate and (R)-2-phosphomalate, which, presumably, bind to the enzyme in opposite orientations.
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CAS REGISTRY NUMBER
COMMENTARY hide
409095-18-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
(R)-2-phospholactate + H2O
lactate + phosphate
show the reaction diagram
-
-
-
-
?
(S)-2-phospholactate + H2O
lactate + phosphate
show the reaction diagram
-
no activity with (R)-phospholactate
-
-
?
(S)-2-phosphomalate + H2O
malate + phosphate
show the reaction diagram
-
-
-
-
?
2-phospho-3-sulfolactate + H2O
3-sulfolactate + phosphate
show the reaction diagram
-
the enzyme catalyzes the second step in biosynthesis of coenzyme M
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-
?
phosphoglycolate + H2O
glycolate + phosphate
show the reaction diagram
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-
-
-
?
phosphoglycolate + H2O
lactate + phosphate
show the reaction diagram
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-
-
-
?
rac-2-phosphosulfolactate + H2O
sulfolactate + phosphate
show the reaction diagram
additional information
?
-
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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
2-phospho-3-sulfolactate + H2O
3-sulfolactate + phosphate
show the reaction diagram
-
the enzyme catalyzes the second step in biosynthesis of coenzyme M
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-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
can fully substitute for Mg2+
Cu2+
-
weak activation
Mn2+
-
can fully substitute for Mg2+
Ni2+
-
can fully substitute for Mg2+
Zn2+
-
can fully substitute for Mg2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-carboxyethylphosphonate
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weak, polyhistidine-tagged enzyme
Ca2+
-
in presence of equimolar Mg2+, polyhistidine-tagged enzyme
Cd2+
-
in presence of equimolar Mg2+, polyhistidine-tagged enzyme
Cu+
-
in presence of equimolar Mg2+, polyhistidine-tagged enzyme
Fe2+
-
in presence of equimolar Mg2+, polyhistidine-tagged enzyme
Fe3+
-
in presence of equimolar Mg2+, polyhistidine-tagged enzyme
Mg2+
-
in presence of equimolar Mg2+, polyhistidine-tagged enzyme
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011
(R)-phosphomalate
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0.148
(S)-phospholactate
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-
0.009
(S)-phosphomalate
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0.034
Phosphoglycolate
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-
0.063
rac-phosphosulfolactate
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-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48
-
rac-phosphosulfolactate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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polyhistidine-tagged enzyme, hydrolysis of rac-phosphosulfolactate
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7
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pH 4.5: about 80% of maximal activity, pH 7.0: about 55%of maximal activity, polyhistidine-tagged enzyme, hydrolysis of rac-phosphosulfolactate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
-
polyhistidine-tagged enzyme, hydrolysis of rac-phosphosulfolactate
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65 - 85
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65°C: about 50% of maximal activity, 85°C: about 70% of maximal activity, polyhistidine-tagged enzyme, hydrolysis of rac-phosphosulfolactate
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Q97E82
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787);
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26010
gel filtration
30000
-
x * 30000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 30000, SDS-PAGE
dimer
crystallography
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by the nanodroplet vapor diffusion method, at 2.6 A resolution. Belongs to space group C2221 with unit cell parameters a = 46.70, b = 69.19, c = 453.52 A. Model of three ComB monomers (residues 1-235 for chains A, B, and C), three (2R)-3-sulfolactate molecules, and 93 water molecules in the asymmetric unit. ComB is composed of 10 beta-strands, nine alpha-helices and five 310-helices
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-30°C, in presence of 50% v/v glycerol, 25% loss of activity after 3 weeks
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4°C, 7% loss of activity after 3 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
on Ni2+ resin and by gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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into plasmid pMH4, expressed in Escherichia coli strain DL41
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LINKS TO OTHER DATABASES (specific for EC-Number 3.1.3.71)
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)