Identification of Active Site Residues Involved in Metal Cofactor Binding and Stereospecific Substrate Recognition in Mammalian Tyrosinase. Implications to the Catalytic Cycle†

Biochemistry ◽  
2002 ◽  
Vol 41 (2) ◽  
pp. 679-686 ◽  
Author(s):  
Concepción Olivares ◽  
José C. García-Borrón ◽  
Francisco Solano
Keyword(s):  
Active Site ◽  
Substrate Recognition ◽  
Catalytic Cycle ◽  
Active Site Residues ◽  
Cofactor Binding ◽  
Metal Cofactor

Differential Contribution of Active Site Residues in Substrate Recognition Sites 1 and 5 to Cytochrome P450 2C8 Substrate Selectivity and Regioselectivity†

Biochemistry ◽  
2004 ◽  
Vol 43 (24) ◽  
pp. 7834-7842 ◽  
Author(s):  
Oranun Kerdpin ◽  
David J. Elliot ◽  
Sanford L. Boye ◽  
Donald J. Birkett ◽  
Krongtong Yoovathaworn ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Active Site ◽  
Substrate Recognition ◽  
Substrate Selectivity ◽  
Active Site Residues ◽  
Recognition Sites ◽  
Cytochrome P450 2C8 ◽  
Differential Contribution

scholarly journals Structure ofEscherichia coliGrx2 in complex with glutathione: a dual-function hybrid of glutaredoxin and glutathioneS-transferase

2014 ◽  
Vol 70 (7) ◽  
pp. 1907-1913 ◽  
Author(s):  
Jun Ye ◽  
S. Venkadesh Nadar ◽  
Jiaojiao Li ◽  
Barry P. Rosen
Keyword(s):  
Escherichia Coli ◽  
Electron Donor ◽  
Active Site ◽  
Active Sites ◽  
Catalytic Cycle ◽  
Dual Function ◽  
Active Site Residues ◽  
E Coli ◽  
Arsenate Reduction ◽  
Gst Activity

The structure of glutaredoxin 2 (Grx2) fromEscherichia colico-crystallized with glutathione (GSH) was solved at 1.60 Å resolution. The structure of a mutant with the active-site residues Cys9 and Cys12 changed to serine crystallized in the absence of glutathione was solved to 2.4 Å resolution. Grx2 has an N-terminal domain characteristic of glutaredoxins, and the overall structure is congruent with the structure of glutathioneS-transferases (GSTs). Purified Grx2 exhibited GST activity. Grx2, which is the physiological electron donor for arsenate reduction byE. coliArsC, was docked with ArsC. The docked structure could be fitted with GSH bridging the active sites of the two proteins. It is proposed that Grx2 is a novel Grx/GST hybrid that functions in two steps of the ArsC catalytic cycle: as a GST it catalyzes glutathionylation of the ArsC–As(V) intermediate and as a glutaredoxin it catalyzes deglutathionylation of the ArsC–As(III)–SG intermediate.

scholarly journals CYP2E1 active site residues in substrate recognition sequence 5 identified by photoaffinity labeling and homology modeling

2007 ◽  
Vol 459 (1) ◽  
pp. 59-69 ◽  
Author(s):  
Samuel L. Collom ◽  
Arvind P. Jamakhandi ◽  
Alan J. Tackett ◽  
Anna Radominska-Pandya ◽  
Grover P. Miller
Keyword(s):  
Homology Modeling ◽  
Active Site ◽  
Substrate Recognition ◽  
Photoaffinity Labeling ◽  
Active Site Residues ◽  
Recognition Sequence

scholarly journals Characterization of glutamyl-tRNA–dependent dehydratases using nonreactive substrate mimics

2019 ◽  
Vol 116 (35) ◽  
pp. 17245-17250 ◽  
Author(s):  
Ian R. Bothwell ◽  
Dillon P. Cogan ◽  
Terry Kim ◽  
Christopher J. Reinhardt ◽  
Wilfred A. van der Donk ◽  
...  
Keyword(s):  
Amino Acids ◽  
Active Site ◽  
Substrate Recognition ◽  
Peptide Substrate ◽  
Active Site Residues ◽  
Food Preservative ◽  
Linear Peptide ◽  
Development Of Resistance ◽  
Subsequent Elimination

The peptide natural product nisin has been used as a food preservative for 6 decades with minimal development of resistance. Nisin contains the unusual amino acids dehydroalanine and dehydrobutyrine, which are posttranslationally installed by class I lanthipeptide dehydratases (LanBs) on a linear peptide substrate through an unusual glutamyl-tRNA–dependent dehydration of Ser and Thr. To date, little is known about how LanBs catalyze the transfer of glutamate from charged tRNAGlu to the peptide substrate, or how they carry out the subsequent elimination of the peptide-glutamyl adducts to afford dehydro amino acids. Here, we describe the synthesis of inert analogs that mimic substrate glutamyl-tRNAGlu and the glutamylated peptide intermediate, and determine the crystal structures of 2 LanBs in complex with each of these compounds. Mutational studies were used to characterize the function of the glutamylation and glutamate elimination active-site residues identified through the structural analysis. These combined studies provide insights into the mechanisms of substrate recognition, glutamylation, and glutamate elimination by LanBs to effect a net dehydration reaction of Ser and Thr.

scholarly journals Contributions of Unique Active Site Residues of Eukaryotic UDP-Galactopyranose Mutases to Substrate Recognition and Active Site Dynamics

Biochemistry ◽  
2014 ◽  
Vol 53 (49) ◽  
pp. 7794-7804 ◽  
Author(s):  
Isabel Da Fonseca ◽  
Insaf A. Qureshi ◽  
Ritcha Mehra-Chaudhary ◽  
Karina Kizjakina ◽  
John J. Tanner ◽  
...  
Keyword(s):  
Active Site ◽  
Substrate Recognition ◽  
Active Site Residues
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