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Information on EC 2.6.1.117 - L-glutamine-4-(methylsulfanyl)-2-oxobutanoate aminotransferase and Organism(s) Bacillus subtilis and UniProt Accession O31665

for references in articles please use BRENDA:EC2.6.1.117
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IUBMB Comments
A pyridoxal-phosphate protein. The enzyme, found in both prokaryotes and eukaryotes, catalyses the last reaction in a methionine salvage pathway. In mammals this activity is catalysed by the multifunctional glutamine transaminase K (cf. EC 2.6.1.64, glutamine---phenylpyruvate transaminase).
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This record set is specific for:
Bacillus subtilis
UNIPROT: O31665
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
101251438, mtnE, Solyc11g013170, Solyc11g013170.1, YkrV, ZEAMMB73_Zm00001d020696, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
mtnE
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamine:4-(methylsulfanyl)-2-oxobutanoate aminotransferase
A pyridoxal-phosphate protein. The enzyme, found in both prokaryotes and eukaryotes, catalyses the last reaction in a methionine salvage pathway. In mammals this activity is catalysed by the multifunctional glutamine transaminase K (cf. EC 2.6.1.64, glutamine---phenylpyruvate transaminase).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutamine + 4-(methylsulfanyl)-2-oxobutanoate
2-oxoglutaramate + L-methionine
show the reaction diagram
-
-
-
?
additional information
?
-
only L-glutamine is accepted as amino donor
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-
?
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
L-glutamine + 4-(methylsulfanyl)-2-oxobutanoate
2-oxoglutaramate + L-methionine
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-(methylsulfanyl)-2-oxobutanoate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.91
4-(methylsulfanyl)-2-oxobutanoate
pH 7.5, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.32
4-(methylsulfanyl)-2-oxobutanoate
pH 7.5, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.26
4-(methylsulfanyl)-2-oxobutanoate
pH 7.5, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.73
4-(methylsulfanyl)-2-oxobutanoate
pH 7.5, 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Berger, B.; English, S.; Chan, G.; Knodel, M.
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
J. Bacteriol.
185
2418-2431
2003
Bacillus subtilis (O31665), Bacillus subtilis 168 (O31665)
Manually annotated by BRENDA team
Ellens, K.; Richardson, L.; Frelin, O.; Collins, J.; Ribeiro, C.; Hsieh, Y.; Mullen, R.; Hanson, A.
Evidence that glutamine transaminase and omega-amidase potentially act in tandem to close the methionine salvage cycle in bacteria and plants
Phytochemistry
113
160-169
2015
Bacillus subtilis (O31665), Bacillus subtilis 168 (O31665), Solanum lycopersicum, Zea mays (A0A1D6I5Q5)
Manually annotated by BRENDA team