We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2R)-phosphosulfolactate phosphohydrolase
-
-
-
-
phosphosulfolactate phosphohydrolase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2R)-2-phospho-3-sulfolactate + H2O = (2R)-3-sulfolactate + phosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
phosphoric ester hydrolysis
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(R)-2-phospholactate + H2O
lactate + phosphate
-
-
-
-
?
(R)-phosphomalate + H2O
malate + phosphate
-
-
-
-
?
(S)-2-phospholactate + H2O
lactate + phosphate
-
no activity with (R)-phospholactate
-
-
?
(S)-2-phosphomalate + H2O
malate + phosphate
-
-
-
-
?
2-phospho-3-sulfolactate + H2O
3-sulfolactate + phosphate
-
the enzyme catalyzes the second step in biosynthesis of coenzyme M
-
-
?
phosphoglycolate + H2O
glycolate + phosphate
-
-
-
-
?
phosphoglycolate + H2O
lactate + phosphate
-
-
-
-
?
rac-2-phosphosulfolactate + H2O
sulfolactate + phosphate
additional information
?
-
rac-2-phosphosulfolactate + H2O
sulfolactate + phosphate
-
-
-
?
rac-2-phosphosulfolactate + H2O
sulfolactate + phosphate
-
-
-
?
additional information
?
-
residues involved in catalysis and/or binding include Arg29, Asp26, Asp154, Asp155, Thr103, Thr147, and Asn104
-
-
?
additional information
?
-
-
residues involved in catalysis and/or binding include Arg29, Asp26, Asp154, Asp155, Thr103, Thr147, and Asn104
-
-
?
additional information
?
-
-
in presence of (S)-lactate the histidine-tagged enzyme can dephosphorylate phosphoglycolate and produce 2-phospholactate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-phospho-3-sulfolactate + H2O
3-sulfolactate + phosphate
-
the enzyme catalyzes the second step in biosynthesis of coenzyme M
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Co2+
-
can fully substitute for Mg2+
Mn2+
-
can fully substitute for Mg2+
Ni2+
-
can fully substitute for Mg2+
Zn2+
-
can fully substitute for Mg2+
Mg2+
contains two Mg2+ ions in the asymmetric unit
Mg2+
-
dependent on, at a concentration approximately equimolar with substrate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-carboxyethylphosphonate
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.011
(R)-phosphomalate
-
-
0.148
(S)-phospholactate
-
-
0.009
(S)-phosphomalate
-
-
0.034
Phosphoglycolate
-
-
0.063
rac-phosphosulfolactate
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
48
-
rac-phosphosulfolactate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5.5
-
polyhistidine-tagged enzyme, hydrolysis of rac-phosphosulfolactate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4.5 - 7
-
pH 4.5: about 80% of maximal activity, pH 7.0: about 55%of maximal activity, polyhistidine-tagged enzyme, hydrolysis of rac-phosphosulfolactate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
75
-
polyhistidine-tagged enzyme, hydrolysis of rac-phosphosulfolactate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
65 - 85
-
65°C: about 50% of maximal activity, 85°C: about 70% of maximal activity, polyhistidine-tagged enzyme, hydrolysis of rac-phosphosulfolactate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
SwissProt
brenda
-
-
-
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
30000
-
x * 30000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-30°C, in presence of 50% v/v glycerol, 25% loss of activity after 3 weeks
-
4°C, 7% loss of activity after 3 weeks
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
on Ni2+ resin and by gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expression in Escherichia coli
-
into plasmid pMH4, expressed in Escherichia coli strain DL41
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
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
brenda
Select items on the left to see more content.
html completed