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Information on EC 4.2.3.3 - methylglyoxal synthase and Organism(s) Bacillus subtilis and UniProt Accession P42980

for references in articles please use BRENDA:EC4.2.3.3
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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.3 methylglyoxal synthase
IUBMB Comments
Does not act on D-glyceraldehyde 3-phosphate.
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This record set is specific for:
Bacillus subtilis
UNIPROT: P42980
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
mgs, methylglyoxal synthase, methylglyoxal synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methylglyoxal synthetase
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-
-
-
MGS
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-
-
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synthase, methylglyoxal
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
glycerone-phosphate phosphate-lyase (methylglyoxal-forming)
Does not act on D-glyceraldehyde 3-phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
37279-01-9
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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
glycerone phosphate
2-oxopropanal + phosphate
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glycerone phosphate
2-oxopropanal + phosphate
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Crh protein
in the absence of preferred carbon sources, the phosphoprotein Crh is present in the nonphosphorylated state and binds to and thereby inhibits the enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150
wild type enzyme, at pH 7.5 and 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 10% (w/v) PEG 4000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Strep-Tactin column chromatography and Sepharose S75 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dickmanns, A.; Zschiedrich, C.P.; Arens, J.; Parfentev, I.; Gundlach, J.; Hofele, R.; Neumann, P.; Urlaub, H.; Goerke, B.; Ficner, R.; Stuelke, J.
Structural basis for the regulatory interaction of the methylglyoxal synthase MgsA with the carbon flux regulator Crh in Bacillus subtilis
J. Biol. Chem.
293
5781-5792
2018
Bacillus subtilis (P42980), Bacillus subtilis 168 (P42980)
Manually annotated by BRENDA team