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

On the catalytic role of the active site residue E121 of E. coli l-aspartate oxidase

Biochimie ◽  
2010 ◽  
Vol 92 (10) ◽  
pp. 1335-1342 ◽  
Author(s):  
Gabriella Tedeschi ◽  
Simona Nonnis ◽  
Bice Strumbo ◽  
Gabriele Cruciani ◽  
Emanuele Carosati ◽  
...  
Keyword(s):  
Active Site ◽  
Active Site Residue ◽  
E Coli ◽  
Catalytic Role

Role of the conserved active site residue tryptophan-24 of human dihydrofolate reductase as revealed by mutagenesis

Biochemistry ◽  
1991 ◽  
Vol 30 (5) ◽  
pp. 1432-1440 ◽  
Author(s):  
William A. Beard ◽  
James R. Appleman ◽  
Shaoming Huang ◽  
Tavner J. Delcamp ◽  
James H. Freisheim ◽  
...  
Keyword(s):  
Dihydrofolate Reductase ◽  
Active Site ◽  
Active Site Residue ◽  
Human Dihydrofolate Reductase

The key role of a non-active-site residue Met148 on the catalytic efficiency of meta-cleavage product hydrolase BphD

2013 ◽  
Vol 97 (24) ◽  
pp. 10399-10411 ◽  
Author(s):  
Hao Zhou ◽  
Yuanyuan Qu ◽  
Chunlei Kong ◽  
E. Shen ◽  
Jingwei Wang ◽  
...  
Keyword(s):  
Active Site ◽  
Catalytic Efficiency ◽  
Cleavage Product ◽  
Active Site Residue

HPr: a model protein

1995 ◽  
Vol 73 (5-6) ◽  
pp. 219-222
Author(s):  
J. W. Anderson
Keyword(s):  
Structure Function ◽  
Active Center ◽  
Active Site ◽  
Central Component ◽  
Active Site Residue ◽  
Phosphotransferase System ◽  
Function Model ◽  
Model Protein

Histidine-containing protein (HPr) is a central component of the bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS). This brief review covers recent structure–function studies on the active center of this protein: the role of the active center residues in phosphotransfer; the residues contributing to the phosphohydrolysis properties of HPr; and the contribution residues in HPr make to the pKaof the transiently phosphorylated active-site residue, His 15. As well, the potential for HPr to be used as a model protein for studying problems not directly associated with its function in the PTS is discussed.Key words: phosphoenolpyruvate: sugar phosphotransferase system, histidine-containing protein, active center, structure–function, model protein.

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

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.

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