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Literature summary extracted from
- Serine racemases from barley, Hordeum vulgare L., and other plant species represent a distinct eukaryotic group: gene cloning and recombinant protein characterization (2007), Phytochemistry, 68, 1530-1536.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.18 | additional information | the enzyme requires pyridoxal 5'-phosphate and divalent cations such as Ca2+, Mg2+, or Mn2+, but not ATP | Hordeum vulgare |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.1.1.18 | DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Hordeum vulgare |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.18 | Fe2+ | complete inhibition of racemase activity at 1 mM | Hordeum vulgare |  |
| 5.1.1.18 | additional information | no inhibition by EDTA of the racemase activity | Hordeum vulgare | |
| 5.1.1.18 | Ni2+ | - |
Hordeum vulgare | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.18 | Ca2+ | activates 3.8fold at 1 mM | Hordeum vulgare | |
| 5.1.1.18 | Mg2+ | activates 2.9fold at 1 mM, ATP reduces the activation by Mg2+ | Hordeum vulgare | |
| 5.1.1.18 | Mn2+ | activates 3.8fold at 1 mM | Hordeum vulgare | |
| 5.1.1.18 | additional information | the enzyme requires pyridoxal 5'-phosphate and divalent cations such as Ca2+, Mg2+, or Mn2+, but not ATP, effects of metal ions on the enzyme's dehydration activity, overview | Hordeum vulgare |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.18 | 35700 | - |
x * 35700, about, sequence calculation, x * 36000, recombinant enzyme, SDS-PAGE | Hordeum vulgare |
| 5.1.1.18 | 36000 | - |
x * 35700, about, sequence calculation, x * 36000, recombinant enzyme, SDS-PAGE | Hordeum vulgare |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.1.18 | L-serine | Hordeum vulgare | - |
D-serine | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.1.18 | Hordeum vulgare | A5HUN0 | cv. Haruna nijo | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.1.1.18 | recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Hordeum vulgare |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.1.18 | L-serine | - |
Hordeum vulgare | D-serine | - |
r | |
| 5.1.1.18 | additional information | the bifunctional enzyme catalyzes not only serine racemization but also dehydration of serine to pyruvate | Hordeum vulgare | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.1.1.18 | ? | x * 35700, about, sequence calculation, x * 36000, recombinant enzyme, SDS-PAGE | Hordeum vulgare |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.18 | 37 | - |
assay at | Hordeum vulgare |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.18 | 8.5 | - |
assay at | Hordeum vulgare |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.18 | pyridoxal 5'-phosphate | bound by Lys67, Phe66, Gly246, Ser322, and Asn94 | Hordeum vulgare | |
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