Cloned (Comment) | Organism |
---|---|
gene malY, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Latilactobacillus sakei |
Protein Variants | Comment | Organism |
---|---|---|
K233A | site-directed mutagenesis | Latilactobacillus sakei |
Y123A | site-directed mutagenesis | Latilactobacillus sakei |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
150 | - |
D-alanine | pH 10.0, 35°C, recombinant His-tagged enzyme | Latilactobacillus sakei | |
169 | - |
L-alanine | pH 10.0, 35°C, recombinant His-tagged enzyme | Latilactobacillus sakei |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
281000 | - |
recombinant His6-tagged enzyme, gel filtration | Latilactobacillus sakei |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Latilactobacillus sakei | Ls-MalY is a bifunctional amino acid racemase with multiple substrate specificity, both the amino acid racemase and beta-lyase reactions of Ls-MalY are catalyzed at the same active site | ? | - |
? | |
additional information | Latilactobacillus sakei LT-13 | Ls-MalY is a bifunctional amino acid racemase with multiple substrate specificity, both the amino acid racemase and beta-lyase reactions of Ls-MalY are catalyzed at the same active site | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Latilactobacillus sakei | A0A223K4L6 | - |
- |
Latilactobacillus sakei LT-13 | A0A223K4L6 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis, to homogeneity | Latilactobacillus sakei |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | strain LK-145 is isolated from a Japanese sake seller as a high D-amino acid producer, and strain LT-13 is isolated from Moto, a starter of sake, as a low D-amino acid producer, using a medium of amylase digested rice as a carbon source | Latilactobacillus sakei | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-alanine | - |
Latilactobacillus sakei | L-alanine | - |
r | |
L-alanine | - |
Latilactobacillus sakei | D-alanine | - |
r | |
L-alanine | - |
Latilactobacillus sakei LT-13 | D-alanine | - |
r | |
L-arginine | - |
Latilactobacillus sakei | D-arginine | - |
r | |
L-asparagine | - |
Latilactobacillus sakei | D-asparagine | - |
r | |
L-glutamate | - |
Latilactobacillus sakei | D-glutamate | - |
r | |
L-glutamate | - |
Latilactobacillus sakei LT-13 | D-glutamate | - |
r | |
L-glutamine | - |
Latilactobacillus sakei | D-glutamine | - |
r | |
L-histidine | - |
Latilactobacillus sakei | D-histidine | - |
r | |
L-leucine | - |
Latilactobacillus sakei | D-leucine | - |
r | |
L-lysine | - |
Latilactobacillus sakei | D-lysine | - |
r | |
L-Methionine | - |
Latilactobacillus sakei | D-Methionine | - |
r | |
L-Methionine | - |
Latilactobacillus sakei LT-13 | D-Methionine | - |
r | |
L-serine | - |
Latilactobacillus sakei | D-serine | - |
r | |
L-threonine | - |
Latilactobacillus sakei | D-threonine | - |
r | |
L-tryptophan | - |
Latilactobacillus sakei | D-tryptophan | - |
r | |
L-valine | - |
Latilactobacillus sakei | D-valine | - |
r | |
additional information | Ls-MalY is a bifunctional amino acid racemase with multiple substrate specificity, both the amino acid racemase and beta-lyase reactions of Ls-MalY are catalyzed at the same active site | Latilactobacillus sakei | ? | - |
? | |
additional information | enzyme Ls-MalY shows cystathionine beta-lyase (EC 4.4.1.8) and amino acid racemase activity with various amino acids, such as Ala, Arg, Asn, Glu, Gln, His, Leu, Lys, Met, Ser, Thr, Trp, and Val, substrate specificity, overview. L-Tyr and D-Tyr are poor substrates. Thr is only converted from L- to D-Thr, but not vice versa. The epsilon-amino group of Lys233 in the primary structure of Ls-MalY likely bound to pyridoxal 5'-phosphate, and Lys233 is an essential residue for Ls-MalY to catalyze both the amino acid racemase and beta-lyase reactions. Tyr123 is a catalytic residue in the amino acid racemase reaction but strongly affects beta-lyase activity | Latilactobacillus sakei | ? | - |
? | |
additional information | Ls-MalY is a bifunctional amino acid racemase with multiple substrate specificity, both the amino acid racemase and beta-lyase reactions of Ls-MalY are catalyzed at the same active site | Latilactobacillus sakei LT-13 | ? | - |
? | |
additional information | enzyme Ls-MalY shows cystathionine beta-lyase (EC 4.4.1.8) and amino acid racemase activity with various amino acids, such as Ala, Arg, Asn, Glu, Gln, His, Leu, Lys, Met, Ser, Thr, Trp, and Val, substrate specificity, overview. L-Tyr and D-Tyr are poor substrates. Thr is only converted from L- to D-Thr, but not vice versa. The epsilon-amino group of Lys233 in the primary structure of Ls-MalY likely bound to pyridoxal 5'-phosphate, and Lys233 is an essential residue for Ls-MalY to catalyze both the amino acid racemase and beta-lyase reactions. Tyr123 is a catalytic residue in the amino acid racemase reaction but strongly affects beta-lyase activity | Latilactobacillus sakei LT-13 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
homohexamer | 6 * 46000, recombinant His6-tagged enzyme, SDS-PAGE | Latilactobacillus sakei |
More | structural modeling of Ls-MalY, structure comparisons, overview | Latilactobacillus sakei |
Synonyms | Comment | Organism |
---|---|---|
LACBS_00576 | locus name | Latilactobacillus sakei |
MalY | - |
Latilactobacillus sakei |
patB | - |
Latilactobacillus sakei |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
- |
Latilactobacillus sakei |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | 55 | activity range, profile overview | Latilactobacillus sakei |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1830 | - |
D-alanine | pH 10.0, 35°C, recombinant His-tagged enzyme | Latilactobacillus sakei | |
2310 | - |
L-alanine | pH 10.0, 35°C, recombinant His-tagged enzyme | Latilactobacillus sakei |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
10 | - |
- |
Latilactobacillus sakei |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
8.5 | 10.5 | activity range, profile overview | Latilactobacillus sakei |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Latilactobacillus sakei |
General Information | Comment | Organism |
---|---|---|
additional information | structural modeling of Ls-MalY, structure comparisons, overview | Latilactobacillus sakei |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
12.2 | - |
D-alanine | pH 10.0, 35°C, recombinant His-tagged enzyme | Latilactobacillus sakei | |
13.7 | - |
L-alanine | pH 10.0, 35°C, recombinant His-tagged enzyme | Latilactobacillus sakei |