Any feedback?
Literature summary extracted from
- A novel bifunctional amino acid racemase with multiple substrate specificity, malY from Lactobacillus sakei LT-13 Genome-based identification and enzymological characterization (2018), Front. Microbiol., 9, 403 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.4.1.13 | 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 |
| 5.1.1.10 | 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
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.4.1.13 | K233A | site-directed mutagenesis, the mutant is only active with D-Ser, but inactive with L- or D-Cys, and L-Ser, in contrast to the wild-type enzyme | Latilactobacillus sakei |
| 4.4.1.13 | Y123A | site-directed mutagenesis, the mutant shows highly reduced activity with L-Cys compared to the wild-type enzyme, and is active with L-Ser in contrast to wild-type | Latilactobacillus sakei |
| 5.1.1.10 | K233A | site-directed mutagenesis | Latilactobacillus sakei |
| 5.1.1.10 | Y123A | site-directed mutagenesis | Latilactobacillus sakei |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.4.1.13 | 11.5 | - |
L-cysteine | pH 10.0, 35°C, recombinant His-tagged enzyme | Latilactobacillus sakei |  |
| 5.1.1.10 | 150 | - |
D-alanine | pH 10.0, 35°C, recombinant His-tagged enzyme | Latilactobacillus sakei | |
| 5.1.1.10 | 169 | - |
L-alanine | pH 10.0, 35°C, recombinant His-tagged enzyme | Latilactobacillus sakei | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.4.1.13 | 281000 | - |
recombinant His6-tagged enzyme, gel filtration | Latilactobacillus sakei |
| 5.1.1.10 | 281000 | - |
recombinant His6-tagged enzyme, gel filtration | Latilactobacillus sakei |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.4.1.13 | L-cystathionine + H2O | Latilactobacillus sakei | overall reaction | L-homocysteine + pyruvate + NH3 | - |
? | |
| 4.4.1.13 | L-cysteine + H2O | Latilactobacillus sakei | - |
? + NH3 | - |
? | |
| 4.4.1.13 | L-cystine + H2O | Latilactobacillus sakei | - |
? + NH3 | - |
? | |
| 4.4.1.13 | 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 | ? | - |
? | |
| 5.1.1.10 | 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 | ? | - |
? | |
| 5.1.1.10 | 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
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.4.1.13 | Latilactobacillus sakei | A0A223K4L6 | - |
- |
| 4.4.1.13 | Latilactobacillus sakei LT-13 | A0A223K4L6 | - |
- |
| 5.1.1.10 | Latilactobacillus sakei | A0A223K4L6 | - |
- |
| 5.1.1.10 | Latilactobacillus sakei LT-13 | A0A223K4L6 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.4.1.13 | recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis, to homogeneity | Latilactobacillus sakei |
| 5.1.1.10 | 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
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 4.4.1.13 | 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 | - |
| 5.1.1.10 | 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 and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.4.1.13 | L-cystathionine + H2O | overall reaction | Latilactobacillus sakei | L-homocysteine + pyruvate + NH3 | - |
? | |
| 4.4.1.13 | L-cysteine + H2O | - |
Latilactobacillus sakei | ? + NH3 | - |
? | |
| 4.4.1.13 | L-cystine + H2O | - |
Latilactobacillus sakei | ? + NH3 | - |
? | |
| 4.4.1.13 | 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 | ? | - |
? | |
| 4.4.1.13 | additional information | enzyme Ls-MalY shows cystathionine beta-lyase and amino acid racemase activity (EC 5.1.1.10) with various amino acids, such as Ala, Arg, Asn, Glu, Gln, His, Leu, Lys, Met, Ser, Thr, Trp, and Val. The beta-lyase shows activity toward L-Cys, but not toward D-Cys, L-Ser, and D-Ser, substrate specificity, overview. Ls-MalY also shows beta-lyase activity with L-cystine and L-cystathionine. 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 | ? | - |
? | |
| 5.1.1.10 | D-alanine | - |
Latilactobacillus sakei | L-alanine | - |
r | |
| 5.1.1.10 | L-alanine | - |
Latilactobacillus sakei | D-alanine | - |
r | |
| 5.1.1.10 | L-alanine | - |
Latilactobacillus sakei LT-13 | D-alanine | - |
r | |
| 5.1.1.10 | L-arginine | - |
Latilactobacillus sakei | D-arginine | - |
r | |
| 5.1.1.10 | L-asparagine | - |
Latilactobacillus sakei | D-asparagine | - |
r | |
| 5.1.1.10 | L-glutamate | - |
Latilactobacillus sakei | D-glutamate | - |
r | |
| 5.1.1.10 | L-glutamate | - |
Latilactobacillus sakei LT-13 | D-glutamate | - |
r | |
| 5.1.1.10 | L-glutamine | - |
Latilactobacillus sakei | D-glutamine | - |
r | |
| 5.1.1.10 | L-histidine | - |
Latilactobacillus sakei | D-histidine | - |
r | |
| 5.1.1.10 | L-leucine | - |
Latilactobacillus sakei | D-leucine | - |
r | |
| 5.1.1.10 | L-lysine | - |
Latilactobacillus sakei | D-lysine | - |
r | |
| 5.1.1.10 | L-Methionine | - |
Latilactobacillus sakei | D-Methionine | - |
r | |
| 5.1.1.10 | L-Methionine | - |
Latilactobacillus sakei LT-13 | D-Methionine | - |
r | |
| 5.1.1.10 | L-serine | - |
Latilactobacillus sakei | D-serine | - |
r | |
| 5.1.1.10 | L-threonine | - |
Latilactobacillus sakei | D-threonine | - |
r | |
| 5.1.1.10 | L-tryptophan | - |
Latilactobacillus sakei | D-tryptophan | - |
r | |
| 5.1.1.10 | L-valine | - |
Latilactobacillus sakei | D-valine | - |
r | |
| 5.1.1.10 | 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 | ? | - |
? | |
| 5.1.1.10 | 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 | ? | - |
? | |
| 5.1.1.10 | 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 | ? | - |
? | |
| 5.1.1.10 | 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
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.4.1.13 | homohexamer | 6 * 46000, recombinant His6-tagged enzyme, SDS-PAGE | Latilactobacillus sakei |
| 4.4.1.13 | More | structural modeling of Ls-MalY, structure comparisons, overview | Latilactobacillus sakei |
| 5.1.1.10 | homohexamer | 6 * 46000, recombinant His6-tagged enzyme, SDS-PAGE | Latilactobacillus sakei |
| 5.1.1.10 | More | structural modeling of Ls-MalY, structure comparisons, overview | Latilactobacillus sakei |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.4.1.13 | beta-lyase | - |
Latilactobacillus sakei |
| 4.4.1.13 | LACBS_00576 | locus name | Latilactobacillus sakei |
| 4.4.1.13 | MalY | - |
Latilactobacillus sakei |
| 4.4.1.13 | patB | - |
Latilactobacillus sakei |
| 5.1.1.10 | LACBS_00576 | locus name | Latilactobacillus sakei |
| 5.1.1.10 | MalY | - |
Latilactobacillus sakei |
| 5.1.1.10 | patB | - |
Latilactobacillus sakei |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.4.1.13 | 40 | - |
- |
Latilactobacillus sakei |
| 5.1.1.10 | 45 | - |
- |
Latilactobacillus sakei |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.4.1.13 | 20 | 45 | activity range, profile overview | Latilactobacillus sakei |
| 5.1.1.10 | 20 | 55 | activity range, profile overview | Latilactobacillus sakei |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.4.1.13 | 930 | - |
L-cysteine | pH 10.0, 35°C, recombinant His-tagged enzyme | Latilactobacillus sakei | |
| 5.1.1.10 | 1830 | - |
D-alanine | pH 10.0, 35°C, recombinant His-tagged enzyme | Latilactobacillus sakei | |
| 5.1.1.10 | 2310 | - |
L-alanine | pH 10.0, 35°C, recombinant His-tagged enzyme | Latilactobacillus sakei | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.4.1.13 | 10 | - |
- |
Latilactobacillus sakei |
| 5.1.1.10 | 10 | - |
- |
Latilactobacillus sakei |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.4.1.13 | 7.5 | 11.5 | activity range, profile overview | Latilactobacillus sakei |
| 5.1.1.10 | 8.5 | 10.5 | activity range, profile overview | Latilactobacillus sakei |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.4.1.13 | pyridoxal 5'-phosphate | - |
Latilactobacillus sakei | |
| 5.1.1.10 | pyridoxal 5'-phosphate | - |
Latilactobacillus sakei | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.4.1.13 | additional information | structural modeling of Ls-MalY, structure comparisons, overview | Latilactobacillus sakei |
| 5.1.1.10 | additional information | structural modeling of Ls-MalY, structure comparisons, overview | Latilactobacillus sakei |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.4.1.13 | 80.87 | - |
L-cysteine | pH 10.0, 35°C, recombinant His-tagged enzyme | Latilactobacillus sakei | |
| 5.1.1.10 | 12.2 | - |
D-alanine | pH 10.0, 35°C, recombinant His-tagged enzyme | Latilactobacillus sakei | |
| 5.1.1.10 | 13.7 | - |
L-alanine | pH 10.0, 35°C, recombinant His-tagged enzyme | Latilactobacillus sakei | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
