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Literature summary for 1.11.1.7 extracted from

  • Koo, L.S.; Tschirret-Guth, R.A.; Straub, W.E.; Moënne-Loccoz, P.; Loehr, T.M.; Ortiz de Montellano, P.R.
    The active site of the thermophilic CYP119 from Sulfolobus solfataricus (2000), J. Biol. Chem., 275, 14112-14123.
    View publication on PubMed
Search for more literature for 1.11.1.7

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli, wild-type and mutant enzymes Sulfolobus acidocaldarius

Protein Variants

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

Organism UniProt Comment Textmining
Sulfolobus acidocaldarius Q55080
-
-
Sulfolobus acidocaldarius DSM 639 Q55080
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzymes Sulfolobus acidocaldarius

Substrates and Products (Substrate)

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

Synonyms Comment Organism
CYP119
-
 Sulfolobus acidocaldarius
Saci_2081 locus name Sulfolobus acidocaldarius

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Sulfolobus acidocaldarius

Temperature Stability [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 assay at Sulfolobus acidocaldarius