Any feedback?
Literature summary for 5.1.1.21 extracted from
- Discovery of a novel amino acid racemase through exploration of natural variation in Arabidopsis thaliana (2015), Proc. Natl. Acad. Sci. USA, 112, 11726-11731 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene daar1, genotyping, untargeted metabolite profiling and genome-wide association analysis on 440 natural accessions of Arabidopsis thaliana to establish genetic linkages between metabolites and genes, recombinant expression of His-tagged enzyme DAAR1 in Escherichia coli strain Rosetta 2 pLysS. The affinity tag does not affect enzyme activity or stability | Arabidopsis thaliana |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | generation of a T-DNA insertion mutant of gene daar1 leading to highly reduced levels of N-malonyl-D-allo-isoleucine | Arabidopsis thaliana |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 17 | - |
L-isoleucine | recombinant His-tagged enzyme, pH 8.0, 22°C | Arabidopsis thaliana |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-isoleucine | Arabidopsis thaliana | - |
D-isoleucine | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | Q66GM9 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme DAAR1 from Escherichia coli strain Rosetta 2 pLysS by nickel affinity chromatography | Arabidopsis thaliana |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| leaf | - |
Arabidopsis thaliana | - |
Storage Stability
| Storage Stability | Organism |
|---|---|
| purified recombinant His-tagged enzyme, rapid loss of activity at room temperature and when storing the enzyme at 4°C for overnight | Arabidopsis thaliana |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-isoleucine | - |
Arabidopsis thaliana | D-isoleucine | - |
r | |
| L-leucine | 1% of the activity with L-isoleucine | Arabidopsis thaliana | D-leucine | - |
r | |
| L-valine | 5% of the activity with L-isoleucine | Arabidopsis thaliana | D-valine | - |
r | |
| additional information | the enzyme does not require pyridoxal 5'-phosphate for its activity. Compared with Ile, DAAR1 shows 1 and 5% relative activity toward Leu and Val, respectively. DAAR1 shows no activity toward N-acetyl-L-Ile, a commercially available surrogate for N-malonyl-L-Ile, suggesting that DAAR1 does not use a N-derivatized substrate | Arabidopsis thaliana | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| amino acid racemase | - |
Arabidopsis thaliana |
| D-amino acid racemase | - |
Arabidopsis thaliana |
| DAAR1 | - |
Arabidopsis thaliana |
| phenazine biosynthesis PhzC/PhzF family protein | UniProt | Arabidopsis thaliana |
| PLP-independent racemase | - |
Arabidopsis thaliana |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at room temperature | Arabidopsis thaliana |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 11.03 | - |
L-isoleucine | recombinant His-tagged enzyme, pH 8.0, 22°C | Arabidopsis thaliana | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Arabidopsis thaliana |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | enzyme does not require pyridoxal 5'-phosphate for its activity | Arabidopsis thaliana |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme is a eukaryotic member of a large and widely conserved phenazine biosynthesis protein PhzF-like protein family and belongs to a D-amino acid racemase gene family. The phenazine biosynthesis-like protein family (PF02567), which is closely related to the DAP epimerase (PF01678), proline racemase (PF05544), and PrpF (PF04303) families | Arabidopsis thaliana |
| malfunction | a daar1 enzyme knockout mutant shows highly reduced levels of N-malonyl-D-allo-isoleucine | Arabidopsis thaliana |
| additional information | exploitation of natural metabolic variation by integrating metabolomics with genome-wide association as an approach for functional genomics study of specialized metabolism | Arabidopsis thaliana |
| physiological function | the amino acid racemase is responsible for the biosynthesis of N-malonyl-D-allo-isoleucine. DAAR1 does not use a N-derivatized substrate and the malonylation of D-amino acids occurs downstream in the metabolic pathway | Arabidopsis thaliana |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.65 | - |
L-isoleucine | recombinant His-tagged enzyme, pH 8.0, 22°C | Arabidopsis thaliana | |
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
