Crystallization (Comment) | Organism |
---|---|
enzyme mutant D40N bound to phenolate, X-ray diffraction structure determination and analysis at 1.25 A resolution | Pseudomonas putida |
Protein Variants | Comment | Organism |
---|---|---|
D103A | site-directed mutagenesis of the catalytic residue, the mutant shows 5000fold reduced activity compared tot he wild-type enzyme | Comamonas testosteroni |
D40N | site-directed mutagenesis, the mutation mimics the protonated aspartate found in the intermediate and equilenin complexes and leads to tighter binding of phenolate and other intermediate analogs | Pseudomonas putida |
D40N | site-directed mutagenesis, the mutation mimics the protonated aspartate found in the intermediate and equilenin complexes and leads to tighter binding of phenolate and other intermediate analogs | Comamonas testosteroni |
Y16F | site-directed mutagenesis of the catalytic residue, the mutant shows 50000fold reduced activity compared tot he wild-type enzyme | Comamonas testosteroni |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics | Pseudomonas putida | |
additional information | - |
additional information | kinetics | Comamonas testosteroni |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
a 3-oxo-DELTA5-steroid | Pseudomonas putida | - |
a 3-oxo-DELTA4-steroid | - |
r | |
a 3-oxo-DELTA5-steroid | Comamonas testosteroni | - |
a 3-oxo-DELTA4-steroid | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Comamonas testosteroni | - |
- |
- |
Pseudomonas putida | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
a 3-oxo-DELTA5-steroid = a 3-oxo-DELTA4-steroid | catalytic mechanism, phenolate binding to the oxyanion hole of ketosteroid isomerase via hydrogen bonding, electrostatic contributions and geometric and electrostatic changes, overview, the KSI reaction involves changes in both geometry and charge distribution as the reaction proceeds from its ground state to its intermediate | Pseudomonas putida | |
a 3-oxo-DELTA5-steroid = a 3-oxo-DELTA4-steroid | catalytic mechanism, phenolate binding to the oxyanion hole of ketosteroid isomerase via hydrogen bonding, electrostatic contributions and geometric and electrostatic changes, overview, the KSI reaction involves changes in both geometry and charge distribution as the reaction proceeds from its ground state to its intermediate, Tyr16 and Asp103 are important in catalysis | Comamonas testosteroni |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
a 3-oxo-DELTA5-steroid | - |
Pseudomonas putida | a 3-oxo-DELTA4-steroid | - |
r | |
a 3-oxo-DELTA5-steroid | - |
Comamonas testosteroni | a 3-oxo-DELTA4-steroid | - |
r | |
a 3-oxo-DELTA5-steroid | phenolates binding to the oxyanion hole of the enzyme via electrostatic interactions, different binding of transition state analogue and substrate, hydrogen bonds shorten with increasing charge localization, overview | Comamonas testosteroni | a 3-oxo-DELTA4-steroid | - |
r | |
a 3-oxo-DELTA5-steroid | phenolates binding to the oxyanion hole of the enzyme via hydrogen bonding, different binding of transition state analogue and substrate, hydrogen bonds shorten with increasing charge localization, overview | Pseudomonas putida | a 3-oxo-DELTA4-steroid | - |
r | |
additional information | equilenin geometrically and electrostatically resembles the dienolate reaction intermediate and transition state, binding structure to enzyme mutant D40N, overview | Comamonas testosteroni | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ketosteroid isomerase | - |
Pseudomonas putida |
ketosteroid isomerase | - |
Comamonas testosteroni |
KSI | - |
Pseudomonas putida |
KSI | - |
Comamonas testosteroni |