Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.3.71 - 2-phosphosulfolactate phosphatase and Organism(s) Clostridium acetobutylicum and UniProt Accession Q97E82

for references in articles please use BRENDA:EC3.1.3.71
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.71 2-phosphosulfolactate phosphatase
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Clostridium acetobutylicum
UNIPROT: Q97E82
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Clostridium acetobutylicum
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
phosphosulfolactate phosphohydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(2R)-phosphosulfolactate phosphohydrolase
-
-
-
-
ComB phosphatase
-
-
-
-
phosphosulfolactate phosphohydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoric ester hydrolysis
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
contains two Mg2+ ions in the asymmetric unit
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
on Ni2+ resin and by gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into plasmid pMH4, expressed in Escherichia coli strain DL41
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team