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Literature summary for 1.4.1.1 extracted from

  • Kato, S.i.; Ohshima, T.; Galkin, A.; Kulakova, L.; Yoshimura, T.; Esaki, N.
    Purification and characterization of alanine dehydrogenase from a marine bacterium,Vibrio proteolyticus (2003), J. Mol. Catal. B, 23, 373-378.
No PubMed abstract available
Search for more literature for 1.4.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli TG1 with a vector plasmid, pUC118 Vibrio proteolyticus

General Stability

General Stability Organism
RbCl and NaCl, significantly stabilize the enzyme. LiCl and KCl stabilize to a lower degree Vibrio proteolyticus

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
 Vibrio proteolyticus
HgCl2 1 mM, complete inhibition Vibrio proteolyticus
methyl p-nitrobenzenesulfonate 0.1 mM, complete inhibition Vibrio proteolyticus
Pb2+
-
 Vibrio proteolyticus
PCMB 0.1 mM, 97% inhibition Vibrio proteolyticus
Sn2+
-
 Vibrio proteolyticus
SO42-
-
 Vibrio proteolyticus
Zn2+
-
 Vibrio proteolyticus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.09
-
 NADH 25°C Vibrio proteolyticus
0.18
-
 NAD+ 25°C Vibrio proteolyticus
0.61
-
 pyruvate 25°C Vibrio proteolyticus
30
-
 L-Ala 25°C Vibrio proteolyticus
110
-
 NH3 25°C Vibrio proteolyticus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
 6 * 40000, SDS-PAGE Vibrio proteolyticus
230000
-
 gel filtration Vibrio proteolyticus

Organism

Organism UniProt Comment Textmining
Vibrio proteolyticus O85596 DSM 30189
-

Purification (Commentary)

Purification (Comment) Organism
-
 Vibrio proteolyticus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
150
-
-
 Vibrio proteolyticus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-fluoropyruvate + NH3 + NADH 74% of the activity with pyruvate Vibrio proteolyticus ? + H2O + NAD+
-
 ?
3-hydroxypyruvate + NH3 + NADH 54% of the activity with pyruvate Vibrio proteolyticus L-Ser + H2O + NAD+
-
 ?
pyruvate + NH3 + NADH
-
 Vibrio proteolyticus L-Ala + H2O + NAD+
-
 r

Subunits

Subunits Comment Organism
hexamer 6 * 40000, SDS-PAGE Vibrio proteolyticus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 pH 7.2, 60 min, stable Vibrio proteolyticus
55
-
 pH 7.2, 60 min, 70% loss of activity Vibrio proteolyticus
65
-
 60 min in presence of 2.0 M NaCl, enzyme retains more than 90% of its activity, 98% of its activity is lost in absence of NaCl Vibrio proteolyticus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 reductive amination of pyruvate Vibrio proteolyticus
10 10.3 oxidative deamination of L-Ala Vibrio proteolyticus

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 9.5 25°C, 10 min, no effect Vibrio proteolyticus

Cofactor

Cofactor Comment Organism Structure
NAD+ no activity with NADP+ Vibrio proteolyticus
NADH no activity with NADPH Vibrio proteolyticus