A theoretical study of hydrolysis by phospholipase A2: the catalytic role of the active site and substrate specificity

1990 ◽  
pp. 1259 ◽  
Author(s):  
Bohdan Waszkowycz ◽  
Ian H. Hillier ◽  
Nigel Gensmantel ◽  
David W. Payling
Keyword(s):  
Substrate Specificity ◽  
Phospholipase A2 ◽  
Active Site ◽  
Theoretical Study ◽  
Catalytic Role

scholarly journals Catalytic role of the active site histidine of porcine pancreatic phospholipase A2 probed by the variants H48Q, H48N and H48K

1999 ◽  
Vol 12 (6) ◽  
pp. 497-503 ◽  
Author(s):  
Marcel J.W. Janssen ◽  
Wendy A.E.C. van de Wiel ◽  
Sigrid H.W. Beiboer ◽  
Muriel D. van Kampen ◽  
Hubertus M. Verheij ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Active Site ◽  
Pancreatic Phospholipase ◽  
Pancreatic Phospholipase A2 ◽  
Catalytic Role ◽  
Active Site Histidine

scholarly journals Structural Characterization of an S-enantioselective Imine Reductase from Mycobacterium Smegmatis

Biomolecules ◽  
2020 ◽  
Vol 10 (8) ◽  
pp. 1130
Author(s):  
Timo Meyer ◽  
Nadine Zumbrägel ◽  
Christina Geerds ◽  
Harald Gröger ◽  
Hartmut H. Niemann
Keyword(s):  
Substrate Specificity ◽  
Active Site ◽  
Mycobacterium Smegmatis ◽  
Catalytic Mechanism ◽  
Building Blocks ◽  
Secondary Amines ◽  
Hydrophobic Amino Acids ◽  
High Degree

NADPH-dependent imine reductases (IREDs) are enzymes capable of enantioselectively reducing imines to chiral secondary amines, which represent important building blocks in the chemical and pharmaceutical industry. Since their discovery in 2011, many previously unknown IREDs have been identified, biochemically and structurally characterized and categorized into families. However, the catalytic mechanism and guiding principles for substrate specificity and stereoselectivity remain disputed. Herein, we describe the crystal structure of S-IRED-Ms from Mycobacterium smegmatis together with its cofactor NADPH. S-IRED-Ms belongs to the S-enantioselective superfamily 3 (SFam3) and is the first IRED from SFam3 to be structurally described. The data presented provide further evidence for the overall high degree of structural conservation between different IREDs of various superfamilies. We discuss the role of Asp170 in catalysis and the importance of hydrophobic amino acids in the active site for stereospecificity. Moreover, a separate entrance to the active site, potentially functioning according to a gatekeeping mechanism regulating access and, therefore, substrate specificity is described.

The catalytic role of the active site aspartic acid in serine proteases

Science ◽  
1987 ◽  
Vol 237 (4817) ◽  
pp. 909-913 ◽  
Author(s):  
C. Craik ◽  
S Roczniak ◽  
C Largman ◽  
W. Rutter
Keyword(s):  
Aspartic Acid ◽  
Active Site ◽  
Serine Proteases ◽  
Catalytic Role

Substrate Specificity in Short-Chain Phospholipid Analogs at the Active Site of Human Synovial Phospholipase A2

1994 ◽  
Vol 37 (24) ◽  
pp. 4118-4129 ◽  
Author(s):  
T. N. Wheeler ◽  
Steven G. Blanchard ◽  
Frank Fang ◽  
Yolanda Gray-Nunez ◽  
Cole O. Harris ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Phospholipase A2 ◽  
Active Site ◽  
Short Chain

Catalytic role of iron-superoxide dismutase in hydrogen abstraction by super oxide radical anion from ascorbic acid

RSC Advances ◽  
2016 ◽  
Vol 6 (89) ◽  
pp. 86650-86662 ◽  
Author(s):  
Manish K. Tiwari ◽  
Phool C. Mishra
Keyword(s):  
Ascorbic Acid ◽  
Superoxide Dismutase ◽  
Active Site ◽  
Radical Anion ◽  
Superoxide Radical ◽  
Hydrogen Abstraction ◽  
Iron Superoxide Dismutase ◽  
Superoxide Radical Anion ◽  
Catalytic Role

The catalytic role of iron-superoxide dismutase (Fe-SOD) in the working of ascorbic acid (AA) as a superoxide radical anion scavenger has been studied by employing a model developed recently for the active site of the enzyme.

A theoretical study on the catalytic role of water in methanol steam reforming on PdZn(111)

2015 ◽  
Vol 5 (5) ◽  
pp. 2935-2944 ◽  
Author(s):  
Zheng-Qing Huang ◽  
Bo Long ◽  
Chun-Ran Chang
Keyword(s):  
Steam Reforming ◽  
Theoretical Study ◽  
Methanol Steam Reforming ◽  
Catalytic Role

The catalytic role of water in the methanol steam reforming process on the PdZn(111) surface is explored theoretically.

Role of active-site residues Tyr55 and Tyr114 in catalysis and substrate specificity ofCorynebacterium diphtheriaeC-S lyase

2014 ◽  
Vol 83 (1) ◽  
pp. 78-90 ◽  
Author(s):  
Alessandra Astegno ◽  
Alessandra Allegrini ◽  
Stefano Piccoli ◽  
Alejandro Giorgetti ◽  
Paola Dominici
Keyword(s):  
Substrate Specificity ◽  
Active Site ◽  
Active Site Residues
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