Crystallization (Comment) | Organism |
---|---|
native apo-enzyme, poor quality of native crystals is resolved by derivatization with selenomethionine, X-ray diffraction structure determination and analysis at 2.94 A resolution, single-wavelength anomalous diffraction methods | Peptoniphilus asaccharolyticus |
Protein Variants | Comment | Organism |
---|---|---|
E243D | site-directed mutagenesis, the enzyme shows impaired NADH binding and catalytic activity due to the disruption of hydrogen bonds with 2'-OH and 3'-OH groups of ribose | Peptoniphilus asaccharolyticus |
E243K | site-directed mutagenesis, the enzyme shows highly impaired NADH binding, inability of E243K to effectively switch to NADPH, which may be explained by the position of the P7 side chain, which is not be ideal for binding to the 2'-phosphate | Peptoniphilus asaccharolyticus |
W244S | site-directed mutagenesis, reduced catalytic activity and altered cofactor specificity, importance of Trp244 is apparent from kinetic studies of W244S | Peptoniphilus asaccharolyticus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate + H2O + NAD+ | Peptoniphilus asaccharolyticus | - |
2-oxoglutarate + NH3 + NADH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Peptoniphilus asaccharolyticus | P28997 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate + H2O + NAD+ | - |
Peptoniphilus asaccharolyticus | 2-oxoglutarate + NH3 + NADH + H+ | - |
r |
Subunits | Comment | Organism |
---|---|---|
hexamer | each polypeptide consists of an N-terminal domain I that adopts an alpha/beta fold with 5 (mixed) beta-strands sandwiched between alpha-helices on both sides. The C-terminal NAD(P)+ binding domain II consists of a modified Rossmann fold with one of the beta-strands in the reverse orientation | Peptoniphilus asaccharolyticus |
Synonyms | Comment | Organism |
---|---|---|
NAD+-specific glutamate dehydrogenase | - |
Peptoniphilus asaccharolyticus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | cofactor recognition and differentiation method, three-dimensional cofactor binding structure, modelling, detailed overview | Peptoniphilus asaccharolyticus | |
NAD+ | - |
Peptoniphilus asaccharolyticus | |
NADH | - |
Peptoniphilus asaccharolyticus |
General Information | Comment | Organism |
---|---|---|
additional information | each polypeptide consists of an N-terminal substrate-binding (domain I) followed by a C-terminal cofactor-binding segment (domain II). The reaction takes place at the junction of the two domains, which move as rigid bodies and are presumed to narrow the cleft during catalysis. Critical glutamate at the P7 position of the core fingerprint with a role in NAD+ binding, mutational and isothermal titration calorimetry studies, overview | Peptoniphilus asaccharolyticus |