Differential Effects of Mutations in Substrate Recognition Site 1 of Cytochrome P450 2C2 on Lauric Acid and Progesterone Hydroxylation

Biochemistry ◽  
1994 ◽  
Vol 33 (26) ◽  
pp. 8029-8034 ◽  
Author(s):  
Petra Straub ◽  
Monica Lloyd ◽  
Eric F. Johnson ◽  
Byron Kemper
Keyword(s):  
Cytochrome P450 ◽  
Lauric Acid ◽  
Substrate Recognition ◽  
Recognition Site ◽  
Differential Effects

scholarly journals Structural Determinants of Aromatase Cytochrome P450 Inhibition in Substrate Recognition Site-1

2002 ◽  
Vol 16 (7) ◽  
pp. 1456-1468 ◽  
Author(s):  
Alan Conley ◽  
Samantha Mapes ◽  
C. Jo Corbin ◽  
Douglas Greger ◽  
Sandra Graham
Keyword(s):  
Cytochrome P450 ◽  
Substrate Recognition ◽  
Recognition Site ◽  
Structural Determinants

Analysis of Substrate Recognition Site 2 (SRS2) in human cytochrome P450 1A2 using whole-plasmid random mutagenesis

2013 ◽  
Vol 9 (1) ◽  
pp. 9-14
Author(s):  
Joohwan Kim ◽  
Songhee Han ◽  
Seunghye Choi ◽  
Hyoung-Goo Park ◽  
Young-Ran Lim ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Substrate Recognition ◽  
Random Mutagenesis ◽  
Recognition Site ◽  
Cytochrome P450 1A2 ◽  
Human Cytochrome

The Role of Cytochrome 2B1 Substrate Recognition Site Residues 115, 294, 297, 298, and 362 in the Oxidation of Steroids and 7-Alkoxycoumarins

2001 ◽  
Vol 394 (1) ◽  
pp. 21-28 ◽  
Author(s):  
Tammy L. Domanski ◽  
You-Qun He ◽  
Emily E. Scott ◽  
Qinmi Wang ◽  
James R. Halpert
Keyword(s):  
Substrate Recognition ◽  
Recognition Site

scholarly journals Specificity and mechanism of carbohydrate demethylation by cytochrome P450 monooxygenases

2018 ◽  
Vol 475 (23) ◽  
pp. 3875-3886 ◽  
Author(s):  
Craig S. Robb ◽  
Lukas Reisky ◽  
Uwe T. Bornscheuer ◽  
Jan-Hendrik Hehemann
Keyword(s):  
Cytochrome P450 ◽  
Active Site ◽  
Substrate Recognition ◽  
High Energy ◽  
Cytochrome P450 Monooxygenases ◽  
P450 Monooxygenases ◽  
High Energy Barrier ◽  
Molecular Determinants ◽  
Cytochrome P450 Family ◽  
Carbohydrate Ligand

Degradation of carbohydrates by bacteria represents a key step in energy metabolism that can be inhibited by methylated sugars. Removal of methyl groups, which is critical for further processing, poses a biocatalytic challenge because enzymes need to overcome a high energy barrier. Our structural and computational analysis revealed how a member of the cytochrome P450 family evolved to oxidize a carbohydrate ligand. Using structural biology, we ascertained the molecular determinants of substrate specificity and revealed a highly specialized active site complementary to the substrate chemistry. Invariance of the residues involved in substrate recognition across the subfamily suggests that they are critical for enzyme function and when mutated, the enzyme lost substrate recognition. The structure of a carbohydrate-active P450 adds mechanistic insight into monooxygenase action on a methylated monosaccharide and reveals the broad conservation of the active site machinery across the subfamily.

Prediction of amino acid residues participated in substrate recognition by cytochrome P450 subfamilies with broad substrate specificity

2013 ◽  
Vol 26 (2) ◽  
pp. 86-91 ◽  
Author(s):  
Maria S. Zharkova ◽  
Boris N. Sobolev ◽  
Nina Yu. Oparina ◽  
Alexander V. Veselovsky ◽  
Alexander I. Archakov
Keyword(s):  
Cytochrome P450 ◽  
Amino Acid ◽  
Substrate Specificity ◽  
Substrate Recognition ◽  
Amino Acid Residues ◽  
Broad Substrate Specificity
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