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

Probing catalytic rate enhancement during intramembrane proteolysis

2016 ◽  
Vol 397 (9) ◽  
pp. 907-919 ◽  
Author(s):  
Elena Arutyunova ◽  
Cameron C. Smithers ◽  
Valentina Corradi ◽  
Adam C. Espiritu ◽  
Howard S. Young ◽  
...  
Keyword(s):  
Active Site ◽  
Serine Proteases ◽  
Homology Model ◽  
Intramembrane Proteolysis ◽  
Oxyanion Hole ◽  
Rate Enhancement ◽  
Transition State Stabilization ◽  
The Family ◽  
Catalytic Dyad

Abstract Rhomboids are ubiquitous intramembrane serine proteases involved in various signaling pathways. While the high-resolution structures of the Escherichia coli rhomboid GlpG with various inhibitors revealed an active site comprised of a serine-histidine dyad and an extensive oxyanion hole, the molecular details of rhomboid catalysis were unclear because substrates are unknown for most of the family members. Here we used the only known physiological pair of AarA rhomboid with its psTatA substrate to decipher the contribution of catalytically important residues to the reaction rate enhancement. An MD-refined homology model of AarA was used to identify residues important for catalysis. We demonstrated that the AarA active site geometry is strict and intolerant to alterations. We probed the roles of H83 and N87 oxyanion hole residues and determined that substitution of H83 either abolished AarA activity or reduced the transition state stabilization energy (ΔΔG‡) by 3.1 kcal/mol; substitution of N87 decreased ΔΔG‡ by 1.6–3.9 kcal/mol. Substitution M154, a residue conserved in most rhomboids that stabilizes the catalytic general base, to tyrosine, provided insight into the mechanism of nucleophile generation for the catalytic dyad. This study provides a quantitative evaluation of the role of several residues important for hydrolytic efficiency and oxyanion stabilization during intramembrane proteolysis.

Kinetic and Structural Studies on the Catalytic Role of the Aspartic Acid Residue Conserved in Copper Amine Oxidase†,‡

Biochemistry ◽  
2006 ◽  
Vol 45 (13) ◽  
pp. 4105-4120 ◽  
Author(s):  
Yen-Chen Chiu ◽  
Toshihide Okajima ◽  
Takeshi Murakawa ◽  
Mayumi Uchida ◽  
Masayasu Taki ◽  
...  
Keyword(s):  
Aspartic Acid ◽  
Amine Oxidase ◽  
Structural Studies ◽  
Copper Amine Oxidase ◽  
Aspartic Acid Residue ◽  
Catalytic Role ◽  
Copper Amine

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.

scholarly journals Analyzing the catalytic role of active site residues in the Fe-type nitrile hydratase from Comamonas testosteroni Ni1

2015 ◽  
Vol 20 (5) ◽  
pp. 885-894 ◽  
Author(s):  
Salette Martinez ◽  
Rui Wu ◽  
Karoline Krzywda ◽  
Veronika Opalka ◽  
Hei Chan ◽  
...  
Keyword(s):  
Active Site ◽  
Nitrile Hydratase ◽  
Comamonas Testosteroni ◽  
Active Site Residues ◽  
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

On the Catalytic Role of the Conserved Active Site Residue His466of Choline Oxidase†

Biochemistry ◽  
2005 ◽  
Vol 44 (3) ◽  
pp. 893-904 ◽  
Author(s):  
Mahmoud Ghanem ◽  
Giovanni Gadda
Keyword(s):  
Active Site ◽  
Choline Oxidase ◽  
Active Site Residue ◽  
Catalytic Role
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