scholarly journals Intramolecular Heme Ligation of the Cytochrome P450 2C9 R108H Mutant Demonstrates Pronounced Conformational Flexibility of the B−C Loop Region: Implications for Substrate Binding

Biochemistry ◽  
2010 ◽  
Vol 49 (40) ◽  
pp. 8700-8708 ◽  
Author(s):  
Arthur G. Roberts ◽  
Matthew J. Cheesman ◽  
Andrew Primak ◽  
Michael K. Bowman ◽  
William M. Atkins ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Substrate Binding ◽  
Conformational Flexibility ◽  
Cytochrome P450 2C9 ◽  
Loop Region ◽  
Heme Ligation

The Substrate Binding Site of Human Liver Cytochrome P450 2C9: An Approach Using Designed Tienilic Acid Derivatives and Molecular Modeling

Biochemistry ◽  
1995 ◽  
Vol 34 (33) ◽  
pp. 10365-10375 ◽  
Author(s):  
Annah Mancy ◽  
Pierre Broto ◽  
Sylvie Dijols ◽  
Patrick M. Dansette ◽  
Daniel Mansuy
Keyword(s):  
Cytochrome P450 ◽  
Molecular Modeling ◽  
Binding Site ◽  
Human Liver ◽  
Substrate Binding ◽  
Cytochrome P450 2C9 ◽  
Tienilic Acid ◽  
Substrate Binding Site ◽  
Liver Cytochrome

The Substrate Binding Site of Human Liver Cytochrome P450 2C9:  An NMR Study†

Biochemistry ◽  
1997 ◽  
Vol 36 (42) ◽  
pp. 12672-12682 ◽  
Author(s):  
Sonia Poli-Scaife ◽  
Roger Attias ◽  
Patrick M. Dansette ◽  
Daniel Mansuy
Keyword(s):  
Cytochrome P450 ◽  
Binding Site ◽  
Human Liver ◽  
Substrate Binding ◽  
Cytochrome P450 2C9 ◽  
Substrate Binding Site ◽  
Liver Cytochrome ◽  
Nmr Study

Role of Cytochrome P450 in Tulip Bulb Probed by Substrate-Binding Studies

1992 ◽  
Vol 36 (1) ◽  
pp. 27-30 ◽  
Author(s):  
Steven L. Kelly ◽  
Aysegul Topal ◽  
Ian Barnett ◽  
Diane E. Kelly ◽  
George A. F. Hendry
Keyword(s):  
Cytochrome P450 ◽  
Substrate Binding ◽  
Binding Studies ◽  
Tulip Bulb

scholarly journals Cytochrome P450 2C9 gene polymorphism in phenytoin induced gingival enlargement: A case report

2013 ◽  
Vol 5 (3) ◽  
pp. 237 ◽  
Author(s):  
Agila Samidorai ◽  
N. S. C. Charles ◽  
S. P. K.Kennedy Babu ◽  
V Ramesh
Keyword(s):  
Cytochrome P450 ◽  
Case Report ◽  
Gene Polymorphism ◽  
Cytochrome P450 2C9 ◽  
Gingival Enlargement

scholarly journals A Conserved Domain Is Crucial for Acceptor Substrate Binding in a Family of Glucosyltransferases

2014 ◽  
Vol 197 (3) ◽  
pp. 510-517 ◽  
Author(s):  
Fan Zhu ◽  
Hua Zhang ◽  
Hui Wu
Keyword(s):  
Bacterial Adhesion ◽  
Substrate Binding ◽  
Molecular Replacement ◽  
Bacterial Sepsis ◽  
Content Type ◽  
Acceptor Substrate ◽  
Loop Region ◽  
Conserved Domain ◽  
Substrate Binding Domain ◽  
Insight Into

Serine-rich repeat glycoproteins (SRRPs) are highly conserved in streptococci and staphylococci. Glycosylation of SRRPs is important for bacterial adhesion and pathogenesis.Streptococcus agalactiaeis the leading cause of bacterial sepsis and meningitis among newborns. Srr2, an SRRP fromS. agalactiaestrain COH1, has been implicated in bacterial virulence. Four genes (gtfA,gtfB,gtfC, and gtfD) located downstream ofsrr2share significant homology with genes involved in glycosylation of other SRRPs. We have shown previously thatgtfAandgtfBencode two glycosyltransferases, GtfA and GtfB, that catalyze the transfer of GlcNAc residues to the Srr2 polypeptide. However, the function of other glycosyltransferases in glycosylation of Srr2 is unknown. In this study, we determined that GtfC catalyzed the direct transfer of glucosyl residues to Srr2-GlcNAc. The GtfC crystal structure was solved at 2.7 Å by molecular replacement. Structural analysis revealed a loop region at the N terminus as a putative acceptor substrate binding domain. Deletion of this domain rendered GtfC unable to bind to its substrate Srr2-GlcNAc, concurrently abolished the glycosyltransferase activity of GtfC, and also altered glycosylation of Srr2. Furthermore, deletion of the corresponding regions from GtfC homologs also abolished their substrate binding and enzymatic activity, indicating that this region is functionally conserved. In summary, we have determined that GtfC is important for the glycosylation of Srr2 and identified a conserved loop region that is crucial for acceptor substrate binding from GtfC homologs in streptococci. These findings shed new mechanistic insight into this family of glycosyltransferases.

scholarly journals Preparation, Characterization, and Substrate Metabolism of Gold-Immobilized Cytochrome P450 2C9

2006 ◽  
Vol 128 (26) ◽  
pp. 8374-8375 ◽  
Author(s):  
Peter M. Gannett ◽  
Jarod Kabulski ◽  
Felio A. Perez ◽  
Zhongyuan Liu ◽  
David Lederman ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome P450 2C9 ◽  
Substrate Metabolism
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