Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.11.1.7 extracted from

  • Tschirret-Guth, R.A.; Koo, L.S.; Hoa, G.H.; Ortiz De Montellano, P.R.
    Reversible pressure deformation of a thermophilic cytochrome P450 enzyme (CYP119) and its active-site mutants (2001), J. Am. Chem. Soc., 123, 3412-3417.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
T213A the mutant enzyme shows an important red-shift of their fluorescence maximum, along with an increased shoulder at 396 nm, significant alteration in the protein structure, causing some of the tryptophan residues to become more solvent accessible Sulfolobus acidocaldarius
T213A/T214A the mutant enzyme shows an important red-shift of their fluorescence maximum, along with an increased shoulder at 396 nm, significant alteration in the protein structure, causing some of the tryptophan residues to become more solvent accessible Sulfolobus acidocaldarius
T213W the fluorescence yield of the T213W mutant enzyme is slightly lower than that of the wild type enzyme Sulfolobus acidocaldarius

General Stability

General Stability Organism
pressure stability of the wild-type enzyme and its active-site Thr213 and Thr214 mutants is investigated. The protein is reversibly inactivated by pressure. At 20°C and pH 6.5, the protein undergoes a reversible P450-to-P420 inactivation with a midpoint at 380 MPa and a reaction volume change of -28 ml/mol. The inactivation transition is retarded, and the absolute reaction volume is decreased by increasing temperature or by mutations that decrease the size of the active site cavity. High pressure affects the tryptophan fluorescence yield, which decreases by about 37% at 480 MPa. The effect is reversible and suggests considerable contraction of the protein. Aerobic decomposition of iron-aryl complexes of the CYP119 T213A mutant under increasing hydrostatic pressure results in variation of the N-arylprotoporphyrin-IX regioisomer (NB:NA:NC:ND) adduct pattern from 39:47:07:07 at 0.1 MPa to 23:36:14:27 at 400 MPa. Preincubation of the protein at 400 MPa followed by complex formation and decomposition give the same regioisomer distribution as untreated protein. Sulfolobus acidocaldarius

Organism

Organism UniProt Comment Textmining
Sulfolobus acidocaldarius Q55080
-
-
Sulfolobus acidocaldarius 7 Q55080
-
-

Synonyms

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