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Information on EC 5.1.1.10 - amino-acid racemase and Organism(s) Escherichia coli and UniProt Accession P03813

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EC Tree
     5 Isomerases
         5.1 Racemases and epimerases
             5.1.1 Acting on amino acids and derivatives
                5.1.1.10 amino-acid racemase
IUBMB Comments
A pyridoxal-phosphate protein.
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This record set is specific for:
Escherichia coli
UNIPROT: P03813
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
amino acid racemase, acl racemase, broad-spectrum amino acid racemase, amino-acid racemase, broad specificity amino acid racemase, gknsaar, n-succinylamino acid racemase, broad-specificity amino acid racemase, broad substrate specificity amino acid racemase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
broad-spectrum amino acid racemase
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PLP-independent amino acid racemase
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L-Amino acid racemase
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-
-
-
Racemase, amino acid
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
racemization
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
amino-acid racemase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9068-61-5
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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
D-homoserine
L-homoserine
show the reaction diagram
high activity with 75% of the activity in the other direction
-
-
r
D-methionine
L-methionine
show the reaction diagram
4.8% activity compared to L-homoserine
-
-
r
L-alanine
D-alanine
show the reaction diagram
0.9% activity compared to L-homoserine
-
-
r
L-aminobutyrate
D-aminobutyrate
show the reaction diagram
4.6% activity compared to L-homoserine
-
-
r
L-asparagine
D-asparagine
show the reaction diagram
4.9% activity compared to L-homoserine
-
-
r
L-glutamine
D-glutamine
show the reaction diagram
0.7% activity compared to L-homoserine
-
-
r
L-histidine
D-histidine
show the reaction diagram
7.9% activity compared to L-homoserine
-
-
r
L-homoserine
D-homoserine
show the reaction diagram
best substrate
-
-
r
L-isoleucine
D-isoleucine
show the reaction diagram
3.9% activity compared to L-homoserine
-
-
r
L-leucine
D-leucine
show the reaction diagram
6.6% activity compared to L-homoserine
-
-
r
L-Methionine
D-Methionine
show the reaction diagram
L-Norleucine
D-Norleucine
show the reaction diagram
1.2% activity compared to L-homoserine
-
-
r
L-Norvaline
D-Norvaline
show the reaction diagram
5.8% activity compared to L-homoserine
-
-
r
L-phenylalanine
D-phenylalanine
show the reaction diagram
0.6% activity compared to L-homoserine
-
-
r
L-serine
D-serine
show the reaction diagram
1.5% activity compared to L-homoserine
-
-
r
L-valine
D-valine
show the reaction diagram
6.2% activity compared to L-homoserine
-
-
r
LL-diaminopimelate
meso-diaminopimelate
show the reaction diagram
0.7% activity compared to L-homoserine
-
-
r
additional information
?
-
enzyme YgeA displays broad substrate specificity but low catalytic activity. YgeA preferentially catalyzes the racemization of homoserine. Histochemic product analysis and quantification by HPLC and spectroscopy
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
pyridoxal 5'-phosphate is not required by the enzyme
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
25.1
D-homoserine
pH 8.5, 37°C, recombinant enzyme
171
L-homoserine
pH 8.5, 37°C, recombinant enzyme
additional information
additional information
kinetics, Hanes-Woolf plots
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
activity range, over 50% of maximal activity at pH 8.0-9.5, profile overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
activity range, activity increases from 25°C to 37°C and is highest at 37°C. Activity decreases from 40°C to 50°C, and is almost absent at 55°C, profile overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
quaternary structure analysis of the enzyme using BN-PAGE, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) pLysS by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ygeA, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) pLysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Miyamoto, T.; Katane, M.; Saitoh, Y.; Sekine, M.; Homma, H.
Identification and characterization of novel broad-spectrum amino acid racemases from Escherichia coli and Bacillus subtilis
Amino Acids
49
1885-1894
2017
Escherichia coli (P03813), Bacillus subtilis (P32960), Bacillus subtilis 168 (P32960), Escherichia coli K-12 / MG1655 (P03813)
Manually annotated by BRENDA team