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Literature summary extracted from
- Inhibition of serine and proline racemases by substrate-product analogues (2014), Bioorg. Med. Chem. Lett., 24, 390-393.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.18 | ATP | - |
Schizosaccharomyces pombe |  |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.1.1.4 | recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Acetoanaerobium sticklandii |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.4 | 1-carboxy-7-azoniabicyclo[2.2.1]heptane | a weak inhibitor | Acetoanaerobium sticklandii | |
| 5.1.1.4 | 7-azabicyclo[2.2.1]heptan-7-ium-1-carboxylate | a weak inhibitor of proline racemase, 29% inhibition at 142.5 mM | Acetoanaerobium sticklandii | |
| 5.1.1.4 | additional information | substrate-product analogue inhibitors of racemases may only be effective when the active site is capacious and/or plastic, or when the inhibitor is sufficiently flexible | Acetoanaerobium sticklandii | |
| 5.1.1.4 | tetrahydro-1H-pyrrolizine-7a(5H)-carboxylate | a bicyclic substrate-product analogue and noncompetitive inhibitor of proline racemase | Acetoanaerobium sticklandii | |
| 5.1.1.18 | alpha-(hydroxymethyl)-L-serine | substrate-product analogue, a modest, linear mixed-type inhibitor of serine racemase | Schizosaccharomyces pombe | |
| 5.1.1.18 | additional information | substrate-product analogue inhibitors of racemases may only be effective when the active site is capacious and/or plastic, or when the inhibitor is sufficiently flexible | Schizosaccharomyces pombe |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.4 | 5.7 | - |
L-proline | pH and temperature not specified in the publication | Acetoanaerobium sticklandii | |
| 5.1.1.18 | 19 | - |
L-serine | pH and temperature not specified in the publication | Schizosaccharomyces pombe | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.18 | Ca2+ | activates | Schizosaccharomyces pombe | |
| 5.1.1.18 | Mg2+ | activates | Schizosaccharomyces pombe | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.1.4 | L-proline | Acetoanaerobium sticklandii | - |
D-proline | - |
r | |
| 5.1.1.18 | L-serine | Schizosaccharomyces pombe | - |
D-serine | - |
? | |
| 5.1.1.18 | additional information | Schizosaccharomyces pombe | the enzyme catalyzes both the racemization and alpha,beta-elimination reaction of L- and D-serine to yield pyruvate and ammonia | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.1.4 | Acetoanaerobium sticklandii | - |
- |
- |
| 5.1.1.18 | Schizosaccharomyces pombe | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.1.1.4 | recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Acetoanaerobium sticklandii |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 5.1.1.18 | L-serine = D-serine | two-base racemization mechanism, overview. The enzyme utilizes a two-base mechanism wherein one enantiospecific Broensted base abstracts the proton from the L-Ser-pyridoxal 5'-phosphate aldimine and the conjugate acid of a second enantiospecific Bronsted base protonates the intermediate to form the D-Ser-pyridoxal 5'-phosphate aldimine, and vice versa | Schizosaccharomyces pombe |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.1.4 | L-proline | - |
Acetoanaerobium sticklandii | D-proline | - |
r | |
| 5.1.1.4 | L-proline | two-base racemization mechanism via an aci-carboxylate intermediate | Acetoanaerobium sticklandii | D-proline | - |
r | |
| 5.1.1.18 | L-serine | - |
Schizosaccharomyces pombe | D-serine | - |
? | |
| 5.1.1.18 | additional information | the enzyme catalyzes both the racemization and alpha,beta-elimination reaction of L- and D-serine to yield pyruvate and ammonia | Schizosaccharomyces pombe | ? | - |
? | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.4 | additional information | the enzyme is not pyridoxal 5'-phosphate-dependent | Acetoanaerobium sticklandii | |
| 5.1.1.18 | pyridoxal 5'-phosphate | dependent on | Schizosaccharomyces pombe | |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.4 | 111 | - |
tetrahydro-1H-pyrrolizine-7a(5H)-carboxylate | pH and temperature not specified in the publication | Acetoanaerobium sticklandii | |
| 5.1.1.18 | 167 | - |
alpha-(hydroxymethyl)-L-serine | pH and temperature not specified in the publication | Schizosaccharomyces pombe | |
IC50 Value
| EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.4 | 67 | - |
pH and temperature not specified in the publication | Acetoanaerobium sticklandii | tetrahydro-1H-pyrrolizine-7a(5H)-carboxylate | |
| 5.1.1.4 | 349 | - |
pH and temperature not specified in the publication | Acetoanaerobium sticklandii | 1-carboxy-7-azoniabicyclo[2.2.1]heptane | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.1.1.4 | additional information | the enzyme is a two-base racemase | Acetoanaerobium sticklandii |
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Release 2023.1 (January 2023)
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