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Literature summary extracted from
- The structure and function of a microbial allantoin racemase reveal the origin and conservation of a catalytic mechanism (2016), Biochemistry, 55, 6421-6432 .
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 5.1.99.3 | in cubic and orthorhombic crystal forms, at 2.10 and 2.15 A resolution, respectively | Pseudomonas fluorescens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.1.99.3 | E78D | mutant shows diminished catalytic activity affecting kcat and KM for both enantiomers | Pseudomonas fluorescens |
| 5.1.99.3 | E78Q | loss of catalytic activity | Pseudomonas fluorescens |
| 5.1.99.3 | additional information | The Pseudomonas protein lacks a cysteine residue (C79 in the Klebsiella pneumoniae AllR sequence) that is essential for the two-base catalytic mechanism of KpAllR. The residue is substituted with glycine | Pseudomonas fluorescens |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.99.3 | 1.1 | - |
(R)-allantoin | wild-type, pH 7.6, temperature not specified in the publication | Pseudomonas fluorescens |  |
| 5.1.99.3 | 2.3 | - |
(R)-allantoin | mutant E78D, pH 7.6, temperature not specified in the publication | Pseudomonas fluorescens | |
| 5.1.99.3 | 2.5 | - |
(S)-allantoin | wild-type, pH 7.6, temperature not specified in the publication | Pseudomonas fluorescens | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.1.99.3 | 55000 | - |
gel filtration | Pseudomonas fluorescens |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.99.3 | Pseudomonas fluorescens | E3SAZ9 | - |
- |
| 5.1.99.3 | Pseudomonas fluorescens DSM 50090 | E3SAZ9 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.99.3 | (R)-allantoin | - |
Pseudomonas fluorescens | (S)-allantoin | - |
r | |
| 5.1.99.3 | (R)-allantoin | - |
Pseudomonas fluorescens DSM 50090 | (S)-allantoin | - |
r | |
| 5.1.99.3 | (S)-allantoin | - |
Pseudomonas fluorescens | (R)-allantoin | - |
r | |
| 5.1.99.3 | (S)-allantoin | - |
Pseudomonas fluorescens DSM 50090 | (R)-allantoin | - |
r | |
| 5.1.99.3 | additional information | Allantoin can undergo racemization through formation of a bicyclic intermediate (faster) or proton exchange at the chiral center (slower). The velocity of the reaction via a bicyclic intermediate is unaffected by the enzyme, whereas the velocity of the reaction via the chiral center is increased by 7 orders of magnitude | Pseudomonas fluorescens | ? | - |
? | |
| 5.1.99.3 | additional information | Allantoin can undergo racemization through formation of a bicyclic intermediate (faster) or proton exchange at the chiral center (slower). The velocity of the reaction via a bicyclic intermediate is unaffected by the enzyme, whereas the velocity of the reaction via the chiral center is increased by 7 orders of magnitude | Pseudomonas fluorescens DSM 50090 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.1.99.3 | AllR | - |
Pseudomonas fluorescens |
| 5.1.99.3 | BFW91_04965 | - |
Pseudomonas fluorescens |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.99.3 | 43 | - |
(R)-allantoin | mutant E78D, pH 7.6, temperature not specified in the publication | Pseudomonas fluorescens | |
| 5.1.99.3 | 57 | - |
(R)-allantoin | wild-type, pH 7.6, temperature not specified in the publication | Pseudomonas fluorescens | |
| 5.1.99.3 | 129 | - |
(S)-allantoin | wild-type, pH 7.6, temperature not specified in the publication | Pseudomonas fluorescens | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.1.99.3 | physiological function | mechanism of racemization involves residue Glu78 acting as a base for the abstraction of the C5 proton of (S)-allantoin and Cys 180 transferring a proton on the opposite side of the allantoin ring. In the stereoinversion of (R)-allantoin, proton abstraction is performed by Cys 180 and reprotonation by Glu 78 | Pseudomonas fluorescens |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.99.3 | 16 | - |
(S)-allantoin | mutant E78D, pH 7.6, temperature not specified in the publication | Pseudomonas fluorescens | |
| 5.1.99.3 | 19 | - |
(R)-allantoin | mutant E78D, pH 7.6, temperature not specified in the publication | Pseudomonas fluorescens | |
| 5.1.99.3 | 52 | - |
(S)-allantoin | wild-type, pH 7.6, temperature not specified in the publication | Pseudomonas fluorescens | |
| 5.1.99.3 | 52 | - |
(R)-allantoin | wild-type, pH 7.6, temperature not specified in the publication | Pseudomonas fluorescens | |
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