Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.4.1.2 extracted from

  • Oliveira, T.; Panjikar, S.; Carrigan, J.B.; Hamza, M.; Sharkey, M.A.; Engel, P.C.; Khan, A.R.
    Crystal structure of NAD+-dependent Peptoniphilus asaccharolyticus glutamate dehydrogenase reveals determinants of cofactor specificity (2012), J. Struct. Biol., 177, 543-552.
    View publication on PubMed
Search for more literature for 1.4.1.2

Crystallization (Commentary)

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

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Peptoniphilus asaccharolyticus P28997
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate + H2O + NAD+
-
 Peptoniphilus asaccharolyticus 2-oxoglutarate + NH3 + NADH + H+
-
 r

Subunits

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

Synonyms Comment Organism
NAD+-specific glutamate dehydrogenase
-
 Peptoniphilus asaccharolyticus

Cofactor

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

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