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Literature summary for 1.4.1.5 extracted from

  • Schriek, S.; Kahmann, U.; Staiger, D.; Pistorius, E.K.; Michel, K.P.
    Detection of an L-amino acid dehydrogenase activity in Synechocystis sp. PCC 6803 (2009), J. Exp. Bot., 60, 1035-1046.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone 0.03 mM, 50% inhibition Synechocystis sp.
CaCl2 0.09 mM, 50% inhibition Synechocystis sp.
CoCl2 0.11 mM, 50% inhibition Synechocystis sp.
dipyridyl 0.01 mM, 50% inhibition Synechocystis sp.
KCN 0.1 mM, 50% inhibition Synechocystis sp.
MgCl2 2 mM inhibits enzymatic activity by 50%, 10 mM MgCl2 completely inhibits enzymatic activity Synechocystis sp.
NaCl 8 mM, 50% inhibition Synechocystis sp.
NaN3 0.1 mM, 50% inhibition Synechocystis sp.
NiCl2 0.09 mM, 50% inhibition Synechocystis sp.
o-phenanthroline 0.05 mM, 50% inhibition Synechocystis sp.
Salicylhydroxamic acid 0.02 mM, 50% inhibition Synechocystis sp.
SrCl2 0.13 mM, 50% inhibition Synechocystis sp.
ZnCl2 0.2 mM, 50% inhibition Synechocystis sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2
-
L-arginine pH 8.5 Synechocystis sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
thylakoid membrane
-
Synechocystis sp. 42651
-

Metals/Ions

Metals/Ions Comment Organism Structure
MgCl2 0.5 mM stimulate activity by 1.7fold Synechocystis sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
51400
-
deduced from amino acid sequence Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp. Q55629 PCC 6803
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycine + H2O + NAD+
-
Synechocystis sp. ? + NH3 + NADH
-
?
L-alanine + H2O + NAD+
-
Synechocystis sp. ? + NH3 + NADH
-
?
L-arginine + H2O + NAD+
-
Synechocystis sp. ? + NH3 + NADH
-
?
L-cysteine + H2O + NAD+ best substrate besides L-arginine Synechocystis sp. 3-mercapto-2-oxopropanoate + NH3 + NADH
-
?
L-glutamate + H2O + NAD+
-
Synechocystis sp. 2-oxoglutarate + NH3 + NADH
-
?
L-glutamine + H2O + NAD+
-
Synechocystis sp. 2-oxoglutaramate + NH3 + NADH
-
?
L-histidine + H2O + NAD+
-
Synechocystis sp. 3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + NADH
-
?
L-isoleucine + H2O + NAD+
-
Synechocystis sp. 3-methyl-2-oxopentanoate + NH3 + NADH
-
?
L-leucine + H2O + NAD+
-
Synechocystis sp. ? + NH3 + NADH
-
?
L-Lysine + H2O + NAD+
-
Synechocystis sp. ? + NH3 + NADH
-
?
L-methionine + H2O + NAD+
-
Synechocystis sp. (4-methylsulfanyl)-2-oxobutanoate + NH3 + NADH
-
?
L-ornithine + H2O + NAD+
-
Synechocystis sp. ? + NH3 + NADH
-
?
L-phenylalanine + H2O + NAD+
-
Synechocystis sp. phenylpyruvate + NH3 + NADH
-
?
L-proline + H2O + NAD+
-
Synechocystis sp. ? + NH3 + NADH
-
?
L-threonine + H2O + NAD+
-
Synechocystis sp. 3-hydroxy-2-oxopropanoate + NH3 + NADH
-
?
L-tryptophan + H2O + NAD+
-
Synechocystis sp. 3-(1H-indol-3-yl)-2-oxopropanoate + NH3 + NADH
-
?
L-tyrosine + H2O + NAD+
-
Synechocystis sp. (4-hydroxyphenyl)pyruvate + NH3 + NADH
-
?
L-valine + H2O + NAD+
-
Synechocystis sp. 3-methyl-2-oxobutanoate + NH3 + NADH
-
?
additional information utilizing toluene-permeabilized cells, an L-amino acid- stimulated O2 uptake became detectable in Synechocystis sp. PCC 6803 in a Clark-type electrode. Enzyme reacts specifically with L-amino acids D-amino acids show no reactivity Synechocystis sp. ?
-
?

Synonyms

Synonyms Comment Organism
L-amino acid dehydrogenase
-
Synechocystis sp.
Slr0782
-
Synechocystis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Synechocystis sp.

Cofactor

Cofactor Comment Organism Structure
FAD
-
Synechocystis sp.

Expression

Organism Comment Expression
Synechocystis sp. slot-blot RNA-DNA hybridization experiments show that the slr0782 mRNA level increases, when cells are grown with L-arginine as compared to the growth of cells with nitrate up