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Literature summary for 1.4.1.8 extracted from

  • Honorat, A.; Monot, F.; Ballerini, D.
    Synthesis of L-alanine and L-valine by enzyme systems from Bacillus megaterium (1990), Enzyme Microb. Technol., 12, 515-520.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
2-oxoisovalerate 65 mM, 50% loss of specific activity Priestia megaterium
CoCl2
-
Priestia megaterium
Cu2+ CuSO4: less inhibition compared with HgCl2 and CoCl2 Priestia megaterium
Hg2+
-
Priestia megaterium
L-valine 10 mM, about 50% loss of specific activity Priestia megaterium
Mn2+ MnCl2: less inhibition compared with HgCl2 and CoCl2 Priestia megaterium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
NADH
-
Priestia megaterium
1.5
-
2-oxoisovalerate
-
Priestia megaterium
153
-
NH4+
-
Priestia megaterium

Organism

Organism UniProt Comment Textmining
Priestia megaterium
-
strain ATCC 39118
-

Purification (Commentary)

Purification (Comment) Organism
-
Priestia megaterium

Specific Activity [micromol/min/mg]

Specific Activity Minimum [┬Ámol/min/mg] Specific Activity Maximum [┬Ámol/min/mg] Comment Organism
7.8
-
-
Priestia megaterium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-2-aminobutyrate + H2O + NAD+ 9% of the activity with L-leucine Priestia megaterium 2-oxobutyrate + NADH + NH3 reductive amination: 28.1% of the activity with 2-oxoisovalerate ?
L-2-aminobutyrate + H2O + NAD+ 9% of the activity with L-leucine Priestia megaterium 2-oxobutyrate + NADH + NH3 reductive amination: 28.1% of the activity with 2-oxoisovalerate r
L-2-aminobutyrate + H2O + NAD+ 9% of the activity with L-leucine Priestia megaterium 2-oxobutyrate + NADH + NH3 2-oxobutyrate is identical with alpha-ketobutyrate ?
L-2-aminobutyrate + H2O + NAD+ 9% of the activity with L-leucine Priestia megaterium 2-oxobutyrate + NADH + NH3 2-oxobutyrate is identical with alpha-ketobutyrate r
L-2-aminobutyrate + H2O + NAD+ L-2-aminobutyrate is identical with L-alpha-aminobutyrate Priestia megaterium 2-oxobutyrate + NADH + NH3 reductive amination: 28.1% of the activity with 2-oxoisovalerate ?
L-2-aminobutyrate + H2O + NAD+ L-2-aminobutyrate is identical with L-alpha-aminobutyrate Priestia megaterium 2-oxobutyrate + NADH + NH3 reductive amination: 28.1% of the activity with 2-oxoisovalerate r
L-2-aminobutyrate + H2O + NAD+ L-2-aminobutyrate is identical with L-alpha-aminobutyrate Priestia megaterium 2-oxobutyrate + NADH + NH3 2-oxobutyrate is identical with alpha-ketobutyrate ?
L-2-aminobutyrate + H2O + NAD+ L-2-aminobutyrate is identical with L-alpha-aminobutyrate Priestia megaterium 2-oxobutyrate + NADH + NH3 2-oxobutyrate is identical with alpha-ketobutyrate r
L-alanine + H2O + NAD+ 3% of the activity with L-valine Priestia megaterium pyruvate + NH3 + NADH reductive amination: 2% of the activity with 2-oxoisovalerate r
L-alanine + H2O + NAD+ 3% of the activity with L-valine Priestia megaterium pyruvate + NH3 + NADH pyruvate is identical with alpha-ketopropanoate and 2-oxopropanoate r
L-isoleucine + H2O + NAD+ 61.3% of the activity with L-leucine Priestia megaterium 3-methyl-2-oxopentanoate + NADH + NH3 2-oxo-3-methylvalerate is identical with alpha-keto-beta-methylpentanoate r
L-isoleucine + H2O + NAD+ 61.3% of the activity with L-leucine Priestia megaterium 3-methyl-2-oxopentanoate + NADH + NH3 reductive amination: 21.9% of the activity with 2-oxoisovalerate r
L-leucine + H2O + NAD+ preferred substrate Priestia megaterium 2-oxoisocaproate + NADH + NH3 2-oxoisocaproate is identical with 2-oxo-4-methylpentanoate, 2-oxoisohexanoate and alpha-ketoisocaproate r
L-leucine + H2O + NAD+ preferred substrate Priestia megaterium 2-oxoisocaproate + NADH + NH3 reductive amination: 21.1% of the activity with 2-oxoisovalerate r
L-norleucine + H2O + NAD+ 4.7% of the activity with L-valine Priestia megaterium 2-oxocaproate + NADH + NH3 reductive amination: 9.7% of the activity with 2-oxoisovalerate r
L-norleucine + H2O + NAD+ 4.7% of the activity with L-valine Priestia megaterium 2-oxocaproate + NADH + NH3 2-oxocaproate is identical with 2-oxohexanoate and alpha-keto-n-hexanoate r
L-norvaline + H2O + NAD+ 47.2% of the activity with L-leucine Priestia megaterium 2-oxovalerate + NH3 + NADH reductive amination: 37% of the activity with 2-oxoisovalerate r
L-norvaline + H2O + NAD+ 47.2% of the activity with L-leucine Priestia megaterium 2-oxovalerate + NH3 + NADH 2-oxovalerate is identical with 2-oxopentanoate and alpha-ketovalerate r
L-valine + NAD(P)+ + H2O NAD+ Priestia megaterium 2-oxoisovalerate + NH3 + NAD(P)H NADH r
L-valine + NAD(P)+ + H2O NAD+ Priestia megaterium 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O NAD+ Priestia megaterium 2-oxoisovalerate + NH3 + NAD(P)H reductive amination: preferred substrate r
L-valine + NAD(P)+ + H2O 88.9% of the activity with L-leucine Priestia megaterium 2-oxoisovalerate + NH3 + NAD(P)H NADH r
L-valine + NAD(P)+ + H2O 88.9% of the activity with L-leucine Priestia megaterium 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O 88.9% of the activity with L-leucine Priestia megaterium 2-oxoisovalerate + NH3 + NAD(P)H reductive amination: preferred substrate r
additional information no activity with the D-isomers of the substrates Priestia megaterium additional information
-
?

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
47
-
-
Priestia megaterium

Temperature Stability [┬░C]

Temperature Stability Minimum [┬░C] Temperature Stability Maximum [┬░C] Comment Organism
30
-
0.75 M ammonia buffer pH 8.5, half-life: 12 days Priestia megaterium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
reductive amination Priestia megaterium
10.5
-
oxidative deamination of L-valine Priestia megaterium

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Priestia megaterium
NADH NADH could not be replaced with NADPH for the reductive amination Priestia megaterium