1.4.1.3: glutamate dehydrogenase [NAD(P)+]

This is an abbreviated version!
For detailed information about glutamate dehydrogenase [NAD(P)+], go to the full flat file.

Reaction

Synonyms

At5g07440, At5g18170, dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)), dual-coenzyme specific glutamate dehydrogenase, GDH, gdh-1, GDH1, GDH2, GDH3, GdhA, gdhA_1, GDHB, GDHII, GLDH, GLUD1, GLUD2, GluDH, glutamate dehydrogenase, glutamate dehydrogenase 1, glutamate dehydrogenase 2, glutamic acid dehydrogenase, glutamic dehydrogenase, hGDH1, hGDH2, hGLUD1, hGLUD2, housekeeping glutamate dehydrogenase, L-glutamate dehydrogenase, L-glutamic acid dehydrogenase, Legdh1, Membrane protein 50, MP50, NAD(P)+-dependent glutamate dehydrogenase, NAD(P)-dependent GDH, NAD(P)-dependent glutamate dehydrogenase, NAD(P)-glutamate dehydrogenase, NAD(P)H-dependent glutamate dehydrogenase, NAD(P)H-utilizing glutamate dehydrogenase, NADH-GDH, NADH-glutamate dehydrogenase, TTC1211, TTC1212, TtGDH

ECTree

1 Oxidoreductases

1.4 Acting on the CH-NH₂ group of donors

1.4.1 With NAD⁺ or NADP⁺ as acceptor

1.4.1.3 glutamate dehydrogenase [NAD(P)+]

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Results	in table
91	Activating Compound
1957	AA Sequence
6	Application
1	CAS Registry Number
38	Cloned(Commentary)
184	Cofactor
23	Crystallization (Commentary)
54	Disease/ Diagnostics
1	Expression
36	General Information
13	General Stability
71	IC50 Value
153	Inhibitors
63	Ki Value [mM]
445	KM Value [mM]
42	Localization
7	Metals/Ions
76	Molecular Weight [Da]
30	Natural Substrates/ Products (Substrates)
3	Organic Solvent Stability
185	Organism
11	Pathway
187	PDB ID
73	pH Optimum
12	pH Range
4	pH Stability
2	pI Value
3	Posttranslational Modification
92	Protein Variants
60	Purification (Commentary)
7	Reaction
4	Reaction Type
148	Reference
3	Renatured (Commentary)
139	Source Tissue
67	Specific Activity [micromol/min/mg]
14	Storage Stability
206	Substrates and Products (Substrate)
60	Subunits
118	Synonyms
1	Systematic Name
21	Temperature Optimum [°C]
10	Temperature Range [°C]
49	Temperature Stability [°C]
127	Turnover Number [1/s]

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complete loss of activity after incubation with 6 M guanidine hydrochloride or 7 M urea, no renaturation after dilution into 200 mM phosphate buffer

2 entries

monomeric and oligomeric enzyme show distinct behaviour on guanidine hydrochloride perturbation at neutral pH. The monomer denaturation, although complex, is reversible. Two fluorescent tryptophan classes are detectable in the monomer, monitoring the independent unfolding of two regions through a multistate transition. The oligomeric protein shows a complex denaturation pattern with the tendency to aggregate irreversibly at high denaturant concentration

Saccharolobus solfataricus

718955