Functional Roles of Streptokinase C-Terminal Flexible Peptide in Active Site Formation and Substrate Recognition in Plasminogen Activation†

Biochemistry ◽  
2003 ◽  
Vol 42 (1) ◽  
pp. 114-120 ◽  
Author(s):  
Peng Zhai ◽  
Nancy Wakeham ◽  
Jeffrey A. Loy ◽  
Xuejun C. Zhang
Keyword(s):  
Active Site ◽  
Substrate Recognition ◽  
Site Formation ◽  
Plasminogen Activation ◽  
Functional Roles

scholarly journals Phospholipase A2 Engineering. Structural and Functional Roles of the Highly Conserved Active Site Residue Aspartate-49

Biochemistry ◽  
1994 ◽  
Vol 33 (49) ◽  
pp. 14714-14722 ◽  
Author(s):  
Yishan Li ◽  
Bao-Zhu Yu ◽  
Hongxin Zhu ◽  
Mahendra K. Jain ◽  
Ming-Daw Tsai
Keyword(s):  
Phospholipase A2 ◽  
Active Site ◽  
Active Site Residue ◽  
Functional Roles

Role of active site arginine residues in substrate recognition by PPM1A

2021 ◽  
Author(s):  
Itsumi Tani ◽  
Shogo Ito ◽  
Yukiko Shirahata ◽  
Yutaka Matsuyama ◽  
James G. Omichinski ◽  
...  
Keyword(s):  
Active Site ◽  
Substrate Recognition ◽  
Arginine Residues

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.

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

Folding Mechanism of an Ankyrin Repeat Protein: Scaffold and Active Site Formation of Human CDK Inhibitor p19INK4d

2007 ◽  
Vol 373 (1) ◽  
pp. 219-231 ◽  
Author(s):  
Christian Löw ◽  
Ulrich Weininger ◽  
Markus Zeeb ◽  
Wei Zhang ◽  
Ernest D. Laue ◽  
...  
Keyword(s):  
Active Site ◽  
Ankyrin Repeat ◽  
Site Formation ◽  
Cdk Inhibitor ◽  
Protein Scaffold ◽  
Repeat Protein ◽  
Ankyrin Repeat Protein ◽  
Folding Mechanism

Phospholipase A2 engineering. Structural and functional roles of highly conserved active site residues tyrosine-52 and tyrosine-73

Biochemistry ◽  
1992 ◽  
Vol 31 (28) ◽  
pp. 6402-6413 ◽  
Author(s):  
Cynthia M. Dupureur ◽  
Bao Zhu Yu ◽  
Mahendra K. Jain ◽  
Joseph P. Noel ◽  
Tiliang Deng ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Active Site ◽  
Active Site Residues ◽  
Functional Roles
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