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Information on EC 1.4.99.B3 - L-amino acid dehydrogenase (cytochrome b)
for references in articles please use BRENDA:EC1.4.99.B3preliminary BRENDA-supplied EC number
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1.4.99.B3 L-amino acid dehydrogenase (cytochrome b)Specify your search results
Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
2
cytochrome b
=
an alpha-keto acid
+
+
2
reduced cytochrome b
Synonyms
l-amino acid deaminase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an L-amino acid + H2O + 2 cytochrome b = an alpha-keto acid + NH3 + 2 reduced cytochrome b
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-amino acid:cytochrome b oxidoreductase (deaminating)
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-arginine + H2O + 2 cytochrome b
2-oxo-5-guanidinopentanoic acid + NH3 + 2 reduced cytochrome b
-
-
68% of the activity with L-phenylalanine
-
?
L-Dopa + H2O + 2 cytochrome b
3-(3,4-dihydroxyphenyl)-pyruvate + NH3 + 2 reduced cytochrome b
-
56.7% of the activitywith L-phenylalanine
-
?
L-histidine + H2O + 2 cytochrome b
2-oxo-4-imidazolepropionic acid + NH3 + 2 reduced cytochrome b
-
-
174% of the activity with L-phenylalanine
-
?
L-isoleucine + H2O + 2 cytochrome b
3-methyl-2-oxo-pentanoate + NH3 + 2 reduced cytochrome b
L-methionine + H2O + 2 cytochrome b
4-methylsulfanyl-2-oxobutanoate + NH3 + 2 reduced cytochrome b
L-norleucine + H2O + 2 cytochrome b
2-oxohexanoate + NH3 + 2 reduced cytochrome b
-
-
82% of the activity with L-phenylalanine
-
?
L-ornithine + H2O + 2 cytochrome b
2-oxo-5-aminopentanoate + NH3 + 2 reduced cytochrome b
-
-
73% of the activity with L-phenylalanine
-
?
L-phenylalanine + H2O + 2 cytochrome b
phenylpyruvate + NH3 + 2 reduced cytochrome b
-
-
-
?
L-phenylalanine + H2O + 2 cytochrome c
phenylpyruvate + NH3 + 2 reduced cytochrome c
-
-
acceptor horse cytochrome c
-
?
L-phenylalanine + H2O + 2,6-dichlorophenolindophenol
phenylpyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
-
membrane-free enzyme can be assayed using 2,6-dichlorophenolindophenol as acceptor
-
?
L-phenylalanine + H2O + dichlorophenolindophenol
phenylpyruvate + NH3 + reduced dichlorophenolindophenol
-
-
-
-
?
L-phenylalanine ethyl ester + H2O + 2 cytochrome b
phenylpyruvate ethyl ester + NH3 + 2 reduced cytochrome b
-
33% of the activitywith L-phenylalanine
-
?
L-tryptophan + H2O + 2 cytochrome b
3-(1H-indol-3-yl)-2-oxopropanoic acid + NH3 + 2 reduced cytochrome b
L-cysteine + H2O + 2 cytochrome b
2-oxo-3-thiopropanoate + NH3 + 2 reduced cytochrome b
-
43% of the activitywith L-phenylalanine
-
?
L-cysteine + H2O + 2 cytochrome b
2-oxo-3-thiopropanoate + NH3 + 2 reduced cytochrome b
-
71.5% of the activiy with L-phenylalanine
-
?
L-cysteine + H2O + 2 cytochrome b
2-oxo-3-thiopropanoate + NH3 + 2 reduced cytochrome b
Proteus myxofaciens 4482
-
71.5% of the activiy with L-phenylalanine
-
?
L-isoleucine + H2O + 2 cytochrome b
3-methyl-2-oxo-pentanoate + NH3 + 2 reduced cytochrome b
-
27.8% of the activiy with L-phenylalanine
-
?
L-isoleucine + H2O + 2 cytochrome b
3-methyl-2-oxo-pentanoate + NH3 + 2 reduced cytochrome b
-
43% of the activitywith L-phenylalanine
-
?
L-isoleucine + H2O + 2 cytochrome b
3-methyl-2-oxo-pentanoate + NH3 + 2 reduced cytochrome b
Proteus myxofaciens 4482
-
27.8% of the activiy with L-phenylalanine
-
?
L-leucine + H2O + 2 cytochrome b
2-oxo-4-methylpentanoate + NH3 + 2 reduced cytochrome b
-
-
69% of the activity with L-phenylalanine
-
?
L-leucine + H2O + 2 cytochrome b
2-oxo-4-methylpentanoate + NH3 + 2 reduced cytochrome b
-
111% of the activiy with L-phenylalanine
-
?
L-leucine + H2O + 2 cytochrome b
2-oxo-4-methylpentanoate + NH3 + 2 reduced cytochrome b
-
99.2% of the activitywith L-phenylalanine
-
?
L-leucine + H2O + 2 cytochrome b
2-oxo-4-methylpentanoate + NH3 + 2 reduced cytochrome b
Proteus myxofaciens 4482
-
111% of the activiy with L-phenylalanine
-
?
L-methionine + H2O + 2 cytochrome b
4-methylsulfanyl-2-oxobutanoate + NH3 + 2 reduced cytochrome b
-
-
74% of the activity with L-phenylalanine
-
?
L-methionine + H2O + 2 cytochrome b
4-methylsulfanyl-2-oxobutanoate + NH3 + 2 reduced cytochrome b
-
102% of the activiy with L-phenylalanine
-
?
L-methionine + H2O + 2 cytochrome b
4-methylsulfanyl-2-oxobutanoate + NH3 + 2 reduced cytochrome b
-
86% of the activitywith L-phenylalanine
-
?
L-methionine + H2O + 2 cytochrome b
4-methylsulfanyl-2-oxobutanoate + NH3 + 2 reduced cytochrome b
Proteus myxofaciens 4482
-
102% of the activiy with L-phenylalanine
-
?
L-tryptophan + H2O + 2 cytochrome b
3-(1H-indol-3-yl)-2-oxopropanoic acid + NH3 + 2 reduced cytochrome b
-
60.5% of the activitywith L-phenylalanine
-
?
L-tryptophan + H2O + 2 cytochrome b
3-(1H-indol-3-yl)-2-oxopropanoic acid + NH3 + 2 reduced cytochrome b
-
90.6% of the activiy with L-phenylalanine
-
?
L-tyrosine + H2O + 2 cytochrome b
4-hydroxyphenylpyruvate + NH3 + 2 reduced cytochrome b
-
13.7% of the activitywith L-phenylalanine
-
?
L-tyrosine + H2O + 2 cytochrome b
4-hydroxyphenylpyruvate + NH3 + 2 reduced cytochrome b
-
38.5% of the activiy with L-phenylalanine
-
?
additional information
?
-
-
one mol of phenylpyruvate is produced per half mol O2 used in the reaction. The process is carried on by amino acid specific flavoproteins and cytochromes b1, a1 and a2 of the respiratory chain
-
-
?
additional information
?
-
aliphatic, aromatic or sulfur-containing amino acids are preferred. The reaction has an absolute requirement for O2, releases NH3 and does not produce H2O2
-
-
?
additional information
?
-
the enzyme does not use dioxygen to reoxidize reduced FADH2 and does not produce hydrogen peroxide, instead, it uses a cytochrome b-like protein as an electron acceptor. No substrates: D-amino acids
-
-
?
additional information
?
-
-
the enzyme does not use dioxygen to reoxidize reduced FADH2 and does not produce hydrogen peroxide, instead, it uses a cytochrome b-like protein as an electron acceptor. No substrates: D-amino acids
-
-
?
additional information
?
-
Proteus myxofaciens 4482
aliphatic, aromatic or sulfur-containing amino acids are preferred. The reaction has an absolute requirement for O2, releases NH3 and does not produce H2O2
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no substrate inhibition up to 100 mM L-phenylalanine
-
additional information
-
no substrate inhibition up to 100 mM L-phenylalanine
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
presene of a membrane environment is required for activity
brenda
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
1 * 49900, calculated, recombinant N-terminal deletion mutant
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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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
a deleltion mutant lacking the N-terminal transmembrane alpha-helix, residues 1-27, i almost completely soluble, catalytic activity is below detection
additional information
-
a deleltion mutant lacking the N-terminal transmembrane alpha-helix, residues 1-27, i almost completely soluble, catalytic activity is below detection
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pelmont, J.; Arlaud, G.; Rossat, A.M.
L-Amino acid oxidases of Proteus mirabilis: general properties
Biochimie
54
1359-1374
1972
Proteus mirabilis
brenda
Motta, P.; Molla, G.; Pollegioni, L.; Nardini, M.
Structure-function relationships in L-amino acid deaminase, a flavoprotein belonging to a novel class of biotechnologically relevant enzymes
J. Biol. Chem.
291
10457-75
2016
Proteus myxofaciens (A0A158RFS7), Proteus myxofaciens
brenda
Panataleone, D.P.; Geller, A.M.; Taylor, P.P.
Purification and characterization of an L-amino acid deaminase used to prepare unnatural amino acids
J. Mol. Catal. B
11
795-803
2001
Proteus myxofaciens (A0A158RFS7), Proteus myxofaciens 4482 (A0A158RFS7)
-
brenda
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Release 2023.1 (January 2023)
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