Leucine Dehydrogenase; Chain A, domain 1
Glutamate Dehydrogenase; Chain A, domain 3
Crystallization of an NAD+-dependent glutamate dehydrogenase from Clostridium symbiosum.
The crystal structure of glutamate dehydrogenase from Clostridium symbiosum at 0.6 nm resolution.
Functional studies of a glutamate dehydrogenase with known three-dimensional structure: steady-state kinetics of the forward and reverse reactions catalysed by the NAD(+)-dependent glutamate dehydrogenase of Clostridium symbiosum.
The essential active-site lysines of clostridial glutamate dehydrogenase. A study with pyridoxal-5'-phosphate.
Effect of additives on the crystallization of glutamate dehydrogenase from Clostridium symbiosum. Evidence for a ligand-induced conformational change.
Subunit assembly and active site location in the structure of glutamate dehydrogenase.
Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis.
Evolution of substrate diversity in the superfamily of amino acid dehydrogenases. Prospects for rational chiral synthesis.
Site and significance of chemically modifiable cysteine residues in glutamate dehydrogenase of Clostridium symbiosum and the use of protection studies to measure coenzyme binding.
The catalytic role of aspartate in the active site of glutamate dehydrogenase.
The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures.
Determinants of substrate specificity in the superfamily of amino acid dehydrogenases.
Alteration of the quaternary structure of glutamate dehydrogenase from Clostridium symbiosum by a single mutation distant from the subunit interfaces.
Chemical rescue of the catalytically disabled clostridial glutamate dehydrogenase mutant D165S by fluoride ion.
Amino acid residues involved in the catalytic mechanism of NAD-dependent glutamate dehydrogenase from Halobacterium salinarum.
Identification of lysine residue involved in inactivation of brain glutamate dehydrogenase isoproteins by o-phthalaldehyde.
Insights into the mechanism of domain closure and substrate specificity of glutamate dehydrogenase from Clostridium symbiosum.
Electrochemical study of the effect of ADP and AMP on the kinetics of glutamate dehydrogenase.
A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus.
Construction, separation and properties of hybrid hexamers of glutamate dehydrogenase in which five of the six subunits are contributed by the catalytically inert D165S.
Detection of multiple active site domain motions in transient-state component time courses of the Clostridium symbiosum L-glutamate dehydrogenase-catalyzed oxidative deamination reaction.
This enzyme catalyzes three reactions, dehydrogenation, addition of hydroxyl group to double-bond and elimination accompanied by double-bond formation (see [7]).