Role of Methionine-13 in the Catalytic Mechanism of 6-Phosphogluconate Dehydrogenase from Sheep Liver†

Biochemistry ◽  
2005 ◽  
Vol 44 (7) ◽  
pp. 2432-2440 ◽  
Author(s):  
Carlo Cervellati ◽  
Franco Dallocchio ◽  
Carlo M. Bergamini ◽  
Paul F. Cook
Keyword(s):  
Catalytic Mechanism ◽  
Phosphogluconate Dehydrogenase ◽  
Sheep Liver

scholarly journals Role of Pro-297 in the catalytic mechanism of sheep liver serine hydroxymethyltransferase

2000 ◽  
Vol 350 (3) ◽  
pp. 849 ◽  
Author(s):  
Rashmi TALWAR ◽  
Vijayapandian LEELAVATHY ◽  
Jala V. KRISHNA RAO ◽  
Naropantul APPAJI RAO ◽  
Handanahal S. SAVITHRI
Keyword(s):  
Catalytic Mechanism ◽  
Serine Hydroxymethyltransferase ◽  
Sheep Liver

Role of Lys-226 in the Catalytic Mechanism ofBacillus StearothermophilusSerine HydroxymethyltransferaseCrystal Structure and Kinetic Studies†,‡

Biochemistry ◽  
2005 ◽  
Vol 44 (18) ◽  
pp. 6929-6937 ◽  
Author(s):  
Siddegowda Bhavani ◽  
V. Trivedi ◽  
V. R. Jala ◽  
H. S. Subramanya ◽  
Purnima Kaul ◽  
...  
Keyword(s):  
Catalytic Mechanism ◽  
Kinetic Studies

Study of the catalytic mechanism of a non-heme Fe catalyst: The role of the spin state of the iron

2021 ◽  
Vol 764 ◽  
pp. 138282
Author(s):  
Aikaterini Gemenetzi ◽  
Panagiota Stathi ◽  
Yiannis Deligiannakis ◽  
Maria Louloudi
Keyword(s):  
Spin State ◽  
Catalytic Mechanism ◽  
Fe Catalyst

scholarly journals The nature of carbon dioxide substrate and equilibrium constant of the 6-phosphogluconate dehydrogenase reaction

1969 ◽  
Vol 115 (4) ◽  
pp. 633-638 ◽  
Author(s):  
R. H. Villet ◽  
K. Dalziel
Keyword(s):  
Carbon Dioxide ◽  
Free Energy ◽  
Equilibrium Constant ◽  
Heat Of Reaction ◽  
Phosphogluconate Dehydrogenase ◽  
Sheep Liver ◽  
Dehydrogenase Reaction ◽  
Reductive Carboxylation ◽  
Primary Substrate

1. It was shown that dissolved CO2 and not HCO3− or H2CO3 is the primary substrate for reductive carboxylation with 6-phosphogluconate dehydrogenase from sheep liver. 2. The equilibrium constant of the reaction was measured in solutions of various ionic strengths and at several temperatures, and the free energy and heat of reaction were determined.

Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism

2001 ◽  
Vol 359 (1) ◽  
pp. 65-75 ◽  
Author(s):  
Valeria MENCHISE ◽  
Catherine CORBIER ◽  
Claude DIDIERJEAN ◽  
Michele SAVIANO ◽  
Ettore BENEDETTI ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Proton Transfer ◽  
Chlamydomonas Reinhardtii ◽  
Catalytic Mechanism ◽  
Structural Data ◽  
Careful Analysis ◽  
Wild Type ◽  
Thioredoxin H ◽  
Dynamics Simulations

Thioredoxins are ubiquitous proteins which catalyse the reduction of disulphide bridges on target proteins. The catalytic mechanism proceeds via a mixed disulphide intermediate whose breakdown should be enhanced by the involvement of a conserved buried residue, Asp-30, as a base catalyst towards residue Cys-39. We report here the crystal structure of wild-type and D30A mutant thioredoxin h from Chlamydomonas reinhardtii, which constitutes the first crystal structure of a cytosolic thioredoxin isolated from a eukaryotic plant organism. The role of residue Asp-30 in catalysis has been revisited since the distance between the carboxylate OD1 of Asp-30 and the sulphur SG of Cys-39 is too great to support the hypothesis of direct proton transfer. A careful analysis of all available crystal structures reveals that the relative positioning of residues Asp-30 and Cys-39 as well as hydrophobic contacts in the vicinity of residue Asp-30 do not allow a conformational change sufficient to bring the two residues close enough for a direct proton transfer. This suggests that protonation/deprotonation of Cys-39 should be mediated by a water molecule. Molecular-dynamics simulations, carried out either in vacuo or in water, as well as proton-inventory experiments, support this hypothesis. The results are discussed with respect to biochemical and structural data.

Structure−Function Relationships in Human Glutathione-Dependent Formaldehyde Dehydrogenase. Role of Glu-67 and Arg-368 in the Catalytic Mechanism†,‡

Biochemistry ◽  
2006 ◽  
Vol 45 (15) ◽  
pp. 4819-4830 ◽  
Author(s):  
Paresh C. Sanghani ◽  
Wilhelmina I. Davis ◽  
LanMin Zhai ◽  
Howard Robinson
Keyword(s):  
Structure Function ◽  
Catalytic Mechanism ◽  
Formaldehyde Dehydrogenase

Cloning, Expression, Purification, and Characterization of the 6-Phosphogluconate Dehydrogenase from Sheep Liver

1998 ◽  
Vol 13 (2) ◽  
pp. 251-258 ◽  
Author(s):  
Lilian Chooback ◽  
Nancy E. Price ◽  
William E. Karsten ◽  
John Nelson ◽  
Paula Sundstrom ◽  
...  
Keyword(s):  
Purification And Characterization ◽  
Phosphogluconate Dehydrogenase ◽  
Sheep Liver
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