EC Number | Application | Comment | Organism |
---|---|---|---|
5.1.2.2 | additional information | mandelate racemase from Pseudomonas putida is a promising candidate for the dynamic kinetic resolution of alpha-hydroxy carboxylic acids | Pseudomonas putida |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.8.3.7 | A177P | the mutation is associated with multiple sulfatase deficiency | Homo sapiens |
1.8.3.7 | A279V | the mutation is associated with multiple sulfatase deficiency | Homo sapiens |
1.8.3.7 | A348P | the mutation is associated with multiple sulfatase deficiency | Homo sapiens |
1.8.3.7 | C218Y | the mutation is associated with multiple sulfatase deficiency | Homo sapiens |
1.8.3.7 | C336R | the mutation is associated with multiple sulfatase deficiency | Homo sapiens |
1.8.3.7 | E130D | the mutation is associated with multiple sulfatase deficiency | Homo sapiens |
1.8.3.7 | N259I | the mutation is associated with multiple sulfatase deficiency | Homo sapiens |
1.8.3.7 | P266L | the mutation is associated with multiple sulfatase deficiency | Homo sapiens |
1.8.3.7 | R224W | the mutation is associated with multiple sulfatase deficiency | Homo sapiens |
1.8.3.7 | R345C | the mutation is associated with multiple sulfatase deficiency | Homo sapiens |
1.8.3.7 | R349Q | the mutation is associated with multiple sulfatase deficiency | Homo sapiens |
1.8.3.7 | R349W | the mutation is associated with multiple sulfatase deficiency | Homo sapiens |
1.8.3.7 | S155P | the mutation is associated with multiple sulfatase deficiency | Homo sapiens |
1.8.3.7 | W179S | the mutation is associated with multiple sulfatase deficiency | Homo sapiens |
5.1.2.2 | additional information | evaluation of design of mandelate racemase with higher stability, usage of structural enzyme analysis for reengineering of mandelate racemase for enhanced thermal stability | Pseudomonas putida |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.8.3.7 | a [sulfatase]-L-cysteine + O2 + a thiol | Homo sapiens | - |
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O | - |
? | |
5.1.2.2 | (S)-mandelate | Pseudomonas putida | - |
(R)-mandelate | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.8.3.7 | Homo sapiens | - |
- |
- |
5.1.2.2 | Pseudomonas putida | P11444 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.8.3.7 | a [sulfatase]-L-cysteine + O2 + a thiol | - |
Homo sapiens | a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O | - |
? | |
5.1.2.2 | (S)-mandelate | - |
Pseudomonas putida | (R)-mandelate | - |
r |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.8.3.7 | FGE | - |
Homo sapiens |
5.1.2.2 | mdlA | - |
Pseudomonas putida |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
5.1.2.2 | additional information | - |
the thermal stability of mandelate racemase is investigated through molecular dynamics simulations in the temperature range of 30-90°C, structural alterations at increasing temperatures, overview. Radius of gyration, surface accessibility, and secondary structure content suggest the instability of mandelate racemase at high temperatures | Pseudomonas putida |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.8.3.7 | malfunction | structural distortions due to missense mutations in human formylglycine-generating enzyme lead to multiple sulfatase deficiency | Homo sapiens |
5.1.2.2 | additional information | the thermal stability of mandelate racemase is investigated through molecular dynamics simulations in the temperature range of 30-90°C | Pseudomonas putida |