Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli, wild-type and mutant enzymes | Sulfolobus acidocaldarius |
Protein Variants | Comment | Organism |
---|---|---|
T213A | formation of styrene epoxide is 83% compared to wild-type enzyme. Protein melting temperature is 1.6°C lower compared to wild-type enzyme | Sulfolobus acidocaldarius |
T213A/T214A | formation of styrene epoxide is 1.4fold higher as compared to wild-type enzyme. Protein melting temperature is 3.5°C higher as compared to wild-type enzyme | Sulfolobus acidocaldarius |
T213F | no formation of styrene epoxide. Protein melting temperature is 2.4°C lower compared to wild-type enzyme | Sulfolobus acidocaldarius |
T213S | formation of styrene epoxide is 19% compared to wild-type enzyme. Protein melting temperature is 2°C lower compared to wild-type enzyme | Sulfolobus acidocaldarius |
T213V | formation of styrene epoxide is 0.7% compared to wild-type enzyme. Protein melting temperature is 1.1°C lower compared to wild-type enzyme | Sulfolobus acidocaldarius |
T213W | formation of styrene epoxide is 5% compared to wild-type enzyme. Protein melting temperature is 2.4°C lower compared to wild-type enzyme | Sulfolobus acidocaldarius |
T214A | formation of styrene epoxide is 2.7fold higher as compared to wild-type enzyme. Protein melting temperature is 1.6°C lower compared to wild-type enzyme | Sulfolobus acidocaldarius |
T214V | formation of styrene epoxide is 2.9fold higher as compared to wild-type enzyme. Protein melting temperature is 2.3°C higher as compared to wild-type enzyme. Mutant is separated into two distinct bands during chromatofocusing. The first band contains predominantly low spin protein, and the second band contains predominantly high spin protein | Sulfolobus acidocaldarius |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sulfolobus acidocaldarius | Q55080 | - |
- |
Sulfolobus acidocaldarius DSM 639 | Q55080 | - |
- |
Purification (Comment) | Organism |
---|---|
wild-type and mutant enzymes | Sulfolobus acidocaldarius |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
cis-beta-methylstyrene + H2O | epoxidation takes place with complete retention of the olefin stereochemistry | Sulfolobus acidocaldarius | cis-beta-methylstyrene epoxide + H2O | - |
? | |
cis-beta-methylstyrene + H2O | epoxidation takes place with complete retention of the olefin stereochemistry | Sulfolobus acidocaldarius DSM 639 | cis-beta-methylstyrene epoxide + H2O | - |
? | |
cis-stilbene + H2O | epoxidation takes place with complete retention of the olefin stereochemistry | Sulfolobus acidocaldarius | cis-stilbene epoxide + H2O | - |
? | |
cis-stilbene + H2O | epoxidation takes place with complete retention of the olefin stereochemistry | Sulfolobus acidocaldarius DSM 639 | cis-stilbene epoxide + H2O | - |
? | |
additional information | catalytic mechanism: Thr213 is catalytically important and Thr214 helps to control the iron spin state | Sulfolobus acidocaldarius | ? | - |
? | |
additional information | catalytic mechanism: Thr213 is catalytically important and Thr214 helps to control the iron spin state | Sulfolobus acidocaldarius DSM 639 | ? | - |
? | |
styrene + H2O2 | endogenous electron transfer partners for CYP119 remain unknown, highly unlikely that styrene is the natural substrate for CYP119. Catalytic activity can be assayed in the absence of electron donor proteins using H2O2 as the source of oxidizing equivalents. The enzyme is not able to support styrene epoxidation by putidaredoxin/putidaredoxin reductase | Sulfolobus acidocaldarius | styrene epoxide + H2O | - |
? | |
styrene + H2O2 | endogenous electron transfer partners for CYP119 remain unknown, highly unlikely that styrene is the natural substrate for CYP119. Catalytic activity can be assayed in the absence of electron donor proteins using H2O2 as the source of oxidizing equivalents. The enzyme is not able to support styrene epoxidation by putidaredoxin/putidaredoxin reductase | Sulfolobus acidocaldarius DSM 639 | styrene epoxide + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CYP119 | - |
Sulfolobus acidocaldarius |
Saci_2081 | locus name | Sulfolobus acidocaldarius |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Sulfolobus acidocaldarius |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
protein melting curves indicate that the thermal stability of CYP119 does not depend on the iron spin state or the active site architecture defined by the threonine residues | Sulfolobus acidocaldarius |
80 | - |
catalytic activity is stable to preincubation for 90 min | Sulfolobus acidocaldarius |
87 | - |
protein melting temperature of mutant enzyme T213A/T214A is 87.0°C | Sulfolobus acidocaldarius |
88 | - |
protein melting temperature of mutant enzymes T213F and T213W is 88.1°C | Sulfolobus acidocaldarius |
89 | - |
protein melting temperature of mutant enzymes T213A and T214A is 88.9°C, protein melting temperature of mutant enzyme T213V is 89.4°C, protein melting temperature of mutant enzyme T213S is 88.5°C | Sulfolobus acidocaldarius |
91 | - |
protein melting temperature of wild-type enzyme is 90.5°C | Sulfolobus acidocaldarius |
93 | - |
protein melting temperature of mutant enzyme T214V is 92.8°C | Sulfolobus acidocaldarius |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
assay at | Sulfolobus acidocaldarius |