Information on EC 3.1.3.71 - 2-phosphosulfolactate phosphatase

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

EC NUMBER
COMMENTARY hide
3.1.3.71
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RECOMMENDED NAME
GeneOntology No.
2-phosphosulfolactate phosphatase
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoric ester hydrolysis
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
coenzyme M biosynthesis I
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Methane metabolism
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Microbial metabolism in diverse environments
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coenzyme M biosynthesis
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
409095-18-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
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-
-
-
?
(S)-2-phospholactate + H2O
lactate + phosphate
show the reaction diagram
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no activity with (R)-phospholactate
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-
?
(S)-2-phosphomalate + H2O
malate + phosphate
show the reaction diagram
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-
-
-
?
2-phospho-3-sulfolactate + H2O
3-sulfolactate + phosphate
show the reaction diagram
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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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-
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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
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the enzyme catalyzes the second step in biosynthesis of coenzyme M
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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can fully substitute for Mg2+
Cu2+
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weak activation
Mn2+
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can fully substitute for Mg2+
Ni2+
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can fully substitute for Mg2+
Zn2+
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can fully substitute for Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-carboxyethylphosphonate
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weak, polyhistidine-tagged enzyme
Ca2+
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in presence of equimolar Mg2+, polyhistidine-tagged enzyme
Cd2+
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in presence of equimolar Mg2+, polyhistidine-tagged enzyme
Cu+
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in presence of equimolar Mg2+, polyhistidine-tagged enzyme
Fe2+
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in presence of equimolar Mg2+, polyhistidine-tagged enzyme
Fe3+
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in presence of equimolar Mg2+, polyhistidine-tagged enzyme
Mg2+
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in presence of equimolar Mg2+, polyhistidine-tagged enzyme
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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48
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rac-phosphosulfolactate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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polyhistidine-tagged enzyme, hydrolysis of rac-phosphosulfolactate
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
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polyhistidine-tagged enzyme, hydrolysis of rac-phosphosulfolactate
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
PDB
SCOP
CATH
ORGANISM
UNIPROT
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
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x * 30000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 30000, SDS-PAGE
dimer
crystallography
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
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
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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