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IUBMB Comments 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.
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
(2R)-phosphosulfolactate phosphohydrolase, ComB, ComB phosphatase, phosphosulfolactate phosphohydrolase,
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(2R)-phosphosulfolactate phosphohydrolase
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phosphosulfolactate phosphohydrolase
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(2R)-2-phospho-3-sulfolactate + H2O = (2R)-3-sulfolactate + phosphate
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phosphoric ester hydrolysis
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(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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(R)-2-phospholactate + H2O
lactate + phosphate
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(R)-phosphomalate + H2O
malate + phosphate
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?
(S)-2-phospholactate + H2O
lactate + phosphate
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no activity with (R)-phospholactate
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(S)-2-phosphomalate + H2O
malate + phosphate
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2-phospho-3-sulfolactate + H2O
3-sulfolactate + phosphate
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the enzyme catalyzes the second step in biosynthesis of coenzyme M
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phosphoglycolate + H2O
glycolate + phosphate
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phosphoglycolate + H2O
lactate + phosphate
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rac-2-phosphosulfolactate + H2O
sulfolactate + phosphate
additional information
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rac-2-phosphosulfolactate + H2O
sulfolactate + phosphate
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rac-2-phosphosulfolactate + H2O
sulfolactate + phosphate
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additional information
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residues involved in catalysis and/or binding include Arg29, Asp26, Asp154, Asp155, Thr103, Thr147, and Asn104
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additional information
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residues involved in catalysis and/or binding include Arg29, Asp26, Asp154, Asp155, Thr103, Thr147, and Asn104
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additional information
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in presence of (S)-lactate the histidine-tagged enzyme can dephosphorylate phosphoglycolate and produce 2-phospholactate
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2-phospho-3-sulfolactate + H2O
3-sulfolactate + phosphate
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the enzyme catalyzes the second step in biosynthesis of coenzyme M
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Co2+
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can fully substitute for Mg2+
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+
Mg2+
contains two Mg2+ ions in the asymmetric unit
Mg2+
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dependent on, at a concentration approximately equimolar with substrate
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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
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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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48
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rac-phosphosulfolactate
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5.5
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polyhistidine-tagged enzyme, hydrolysis of rac-phosphosulfolactate
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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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75
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polyhistidine-tagged enzyme, hydrolysis of rac-phosphosulfolactate
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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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SwissProt
brenda
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brenda
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brenda
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30000
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x * 30000, SDS-PAGE
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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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-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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on Ni2+ resin and by gel filtration
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expression in Escherichia coli
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into plasmid pMH4, expressed in Escherichia coli strain DL41
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Graham, D.E.; Graupner, M.; Xu, H.; White, R.H.
Identification of coenzyme M biosynthetic 2-phosphosulfolactate phosphatase. A member of a new class of Mg2+-dependent acid phosphatases
Eur. J. Biochem.
268
5176-5188
2001
Methanocaldococcus jannaschii, Methanosarcina thermophila
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DiDonato, M.; Krishna, S.S.; Schwarzenbacher, R.; McMullan, D.; Agarwalla, S.; Brittain, S.M.; Miller, M.D.; Abdubek, P.; Ambing, E.; Axelrod, H.L.; Canaves, J.M.; Chiu, H.; Deacon, A.M.; Duan, L.; Elsliger, M.; Godzik, A.; Grzechnik, S.K.; Hale, J.; et.al.
Crystal structure of 2-phosphosulfolactate phosphatase (ComB) from Clostridium acetobutylicum at 2.6.A. resolution reveals a new fold with a novel active site
Proteins Struct. Funct. Bioinform.
65
771-776
2006
Clostridium acetobutylicum (Q97E82), Clostridium acetobutylicum
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3.1.3.71 2-phosphosulfolactate phosphatase
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