Information on EC 1.4.99.B3 - L-amino acid dehydrogenase (cytochrome b)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.4.99.B3
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
L-amino acid dehydrogenase (cytochrome b)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an L-amino acid + H2O + 2 cytochrome b = an alpha-keto acid + NH3 + 2 reduced cytochrome b
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
L-amino acid:cytochrome b oxidoreductase (deaminating)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-arginine + H2O + 2 cytochrome b
2-oxo-5-guanidinopentanoic acid + NH3 + 2 reduced cytochrome b
show the reaction diagram
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68% of the activity with L-phenylalanine
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?
L-cysteine + H2O + 2 cytochrome b
2-oxo-3-thiopropanoate + NH3 + 2 reduced cytochrome b
show the reaction diagram
L-Dopa + H2O + 2 cytochrome b
3-(3,4-dihydroxyphenyl)-pyruvate + NH3 + 2 reduced cytochrome b
show the reaction diagram
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56.7% of the activitywith L-phenylalanine
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?
L-histidine + H2O + 2 cytochrome b
2-oxo-4-imidazolepropionic acid + NH3 + 2 reduced cytochrome b
show the reaction diagram
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174% of the activity with L-phenylalanine
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?
L-isoleucine + H2O + 2 cytochrome b
3-methyl-2-oxo-pentanoate + NH3 + 2 reduced cytochrome b
show the reaction diagram
L-leucine + H2O + 2 cytochrome b
2-oxo-4-methylpentanoate + NH3 + 2 reduced cytochrome b
show the reaction diagram
L-methionine + H2O + 2 cytochrome b
4-methylsulfanyl-2-oxobutanoate + NH3 + 2 reduced cytochrome b
show the reaction diagram
L-norleucine + H2O + 2 cytochrome b
2-oxohexanoate + NH3 + 2 reduced cytochrome b
show the reaction diagram
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82% of the activity with L-phenylalanine
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?
L-ornithine + H2O + 2 cytochrome b
2-oxo-5-aminopentanoate + NH3 + 2 reduced cytochrome b
show the reaction diagram
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73% of the activity with L-phenylalanine
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?
L-phenylalanine + H2O + 2 cytochrome b
phenylpyruvate + NH3 + 2 reduced cytochrome b
show the reaction diagram
L-phenylalanine + H2O + 2 cytochrome c
phenylpyruvate + NH3 + 2 reduced cytochrome c
show the reaction diagram
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acceptor horse cytochrome c
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?
L-phenylalanine + H2O + 2,6-dichlorophenolindophenol
phenylpyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
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membrane-free enzyme can be assayed using 2,6-dichlorophenolindophenol as acceptor
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?
L-phenylalanine + H2O + dichlorophenolindophenol
phenylpyruvate + NH3 + reduced dichlorophenolindophenol
show the reaction diagram
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?
L-phenylalanine ethyl ester + H2O + 2 cytochrome b
phenylpyruvate ethyl ester + NH3 + 2 reduced cytochrome b
show the reaction diagram
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33% of the activitywith L-phenylalanine
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?
L-tryptophan + H2O + 2 cytochrome b
3-(1H-indol-3-yl)-2-oxopropanoic acid + NH3 + 2 reduced cytochrome b
show the reaction diagram
L-tyrosine + H2O + 2 cytochrome b
4-hydroxyphenylpyruvate + NH3 + 2 reduced cytochrome b
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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an FAD isoalloxazine ring is exposed to solvent
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no substrate inhibition up to 100 mM L-phenylalanine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.28 - 3.27
L-phenylalanine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.5
L-phenylalanine
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pH 7.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.9
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pH 7.5, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
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negligible activity bleow and above
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
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negligible activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44600
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gel filtration, recombinant N-terminal deletion mutant
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 49900, calculated, recombinant N-terminal deletion mutant
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the overall fold resembles that of known amine or amino acid oxidases. An additional alpha+beta subdomain is placed close to the putative transmembrane alpha-helix and to the active-site entrance, an FAD isoalloxazine ring is exposed to solvent, and a large and accessible active site suits to bind large hydrophobic substrates. The enzyme requires substrate-induced conformational changes of part of the active site, particularly in Arg316 and Phe318, to achieve the correct geometry for catalysis
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
crude extract, 50% residual activity after 24 h at 25°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10% glycerol, 1 month, 50% residual activity
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-80°C, 10% glycerol, 1 month, 75% residual activity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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a deleltion mutant lacking the N-terminal transmembrane alpha-helix, residues 1-27, i almost completely soluble, catalytic activity is below detection