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Literature summary for 1.4.1.2 extracted from

  • Joshi, C.; Pathan, E.; Punekar, N.; Tupe, S.; Kapadnis, B.; Deshpande, M.
    A biochemical correlate of dimorphism in a zygomycete Benjaminiella poitrasii Characterization of purified NAD-dependent glutamate dehydrogenase, a target for antifungal agents (2013), Antonie van Leeuwenhoek, 104, 25-36 .
    View publication on PubMed
Search for more literature for 1.4.1.2

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.06
-
 NADH pH 8.0, 23°C Benjaminiella poitrasii
0.17
-
 NAD+ pH 8.0, 23°C Benjaminiella poitrasii
3.12
-
 2-oxoglutarate pH 8.0, 23°C Benjaminiella poitrasii
27.7
-
 NH4+ pH 8.0, 23°C Benjaminiella poitrasii
33.33
-
 L-glutamate pH 8.0, 23°C Benjaminiella poitrasii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
371000
-
 gel filtration Benjaminiella poitrasii

Organism

Organism UniProt Comment Textmining
Benjaminiella poitrasii
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein enzyme is present in active phosphorylated form in hyphal cells Benjaminiella poitrasii

Purification (Commentary)

Purification (Comment) Organism
-
 Benjaminiella poitrasii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
48.7
-
 pH 8.0, 23°C Benjaminiella poitrasii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + NH3 + NADH + H+ 136% of the activtiy with L-glutamate Benjaminiella poitrasii L-glutamate + H2O + NAD+
-
 r
2-oxoglutarate + NH4+ + NADH
-
 Benjaminiella poitrasii L-glutamate + NAD+
-
 ?
L-glutamate + H2O + NAD+
-
 Benjaminiella poitrasii 2-oxoglutarate + NH3 + NADH + H+
-
 r

Subunits

Subunits Comment Organism
tetramer 4 * 97000, SDS-PAGE Benjaminiella poitrasii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 oxidative deamination Benjaminiella poitrasii
30
-
 reductive amination of 2-oxoglutarate Benjaminiella poitrasii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 reductive amination of 2-oxoglutarate Benjaminiella poitrasii
8.5
-
 oxidative deamination Benjaminiella poitrasii

Cofactor

Cofactor Comment Organism Structure
NAD+ enzyme is specific towards NAD(H) Benjaminiella poitrasii
NADH enzyme is specific towards NAD(H) Benjaminiella poitrasii

pI Value

Organism Comment pI Value Maximum pI Value
Benjaminiella poitrasii isoelectic focusing
-
 5.3