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Literature summary extracted from

  • 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 (2016), J. Biol. Chem., 291, 10457-75.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.99.B3 expression in Escherichia coli Proteus myxofaciens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.4.99.B3 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 Proteus myxofaciens

Protein Variants

EC Number Protein Variants Comment Organism
1.4.99.B3 additional information a deleltion mutant lacking the N-terminal transmembrane alpha-helix, residues 1-27, i almost completely soluble, catalytic activity is below detection Proteus myxofaciens

General Stability

EC Number General Stability Organism
1.4.99.B3 crude extract, 50% residual activity after 24 h at 25°C Proteus myxofaciens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.99.B3 additional information no substrate inhibition up to 100 mM L-phenylalanine Proteus myxofaciens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.99.B3 3.27
-
 L-phenylalanine pH 7.5, 25°C Proteus myxofaciens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.4.99.B3 membrane presene of a membrane environment is required for activity Proteus myxofaciens 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.99.B3 44600
-
 gel filtration, recombinant N-terminal deletion mutant Proteus myxofaciens
1.4.99.B3 49900
-
-
 Proteus myxofaciens

Organism

EC Number Organism UniProt Comment Textmining
1.4.99.B3 Proteus myxofaciens A0A158RFS7
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.99.B3 2.9
-
 pH 7.5, 25°C Proteus myxofaciens

Storage Stability

EC Number Storage Stability Organism
1.4.99.B3 -20°C, 10% glycerol, 1 month, 50% residual activity Proteus myxofaciens
1.4.99.B3 -80°C, 10% glycerol, 1 month, 75% residual activity Proteus myxofaciens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.99.B3 L-cysteine + H2O + 2 cytochrome b
-
 Proteus myxofaciens 2-oxo-3-thiopropanoate + NH3 + 2 reduced cytochrome b 43% of the activitywith L-phenylalanine ?
1.4.99.B3 L-Dopa + H2O + 2 cytochrome b
-
 Proteus myxofaciens 3-(3,4-dihydroxyphenyl)-pyruvate + NH3 + 2 reduced cytochrome b 56.7% of the activitywith L-phenylalanine ?
1.4.99.B3 L-isoleucine + H2O + 2 cytochrome b
-
 Proteus myxofaciens 3-methyl-2-oxo-pentanoate + NH3 + 2 reduced cytochrome b 43% of the activitywith L-phenylalanine ?
1.4.99.B3 L-leucine + H2O + 2 cytochrome b
-
 Proteus myxofaciens 2-oxo-4-methylpentanoate + NH3 + 2 reduced cytochrome b 99.2% of the activitywith L-phenylalanine ?
1.4.99.B3 L-methionine + H2O + 2 cytochrome b
-
 Proteus myxofaciens 4-methylsulfanyl-2-oxobutanoate + NH3 + 2 reduced cytochrome b 86% of the activitywith L-phenylalanine ?
1.4.99.B3 L-phenylalanine + H2O + 2 cytochrome b
-
 Proteus myxofaciens phenylpyruvate + NH3 + 2 reduced cytochrome b
-
 ?
1.4.99.B3 L-phenylalanine + H2O + 2,6-dichlorophenolindophenol
-
 Proteus myxofaciens phenylpyruvate + NH3 + reduced 2,6-dichlorophenolindophenol membrane-free enzyme can be assayed using 2,6-dichlorophenolindophenol as acceptor ?
1.4.99.B3 L-phenylalanine ethyl ester + H2O + 2 cytochrome b
-
 Proteus myxofaciens phenylpyruvate ethyl ester + NH3 + 2 reduced cytochrome b 33% of the activitywith L-phenylalanine ?
1.4.99.B3 L-tryptophan + H2O + 2 cytochrome b
-
 Proteus myxofaciens 3-(1H-indol-3-yl)-2-oxopropanoic acid + NH3 + 2 reduced cytochrome b 60.5% of the activitywith L-phenylalanine ?
1.4.99.B3 L-tyrosine + H2O + 2 cytochrome b
-
 Proteus myxofaciens 4-hydroxyphenylpyruvate + NH3 + 2 reduced cytochrome b 13.7% of the activitywith L-phenylalanine ?
1.4.99.B3 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 Proteus myxofaciens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.4.99.B3 monomer 1 * 49900, calculated, recombinant N-terminal deletion mutant Proteus myxofaciens

Synonyms

EC Number Synonyms Comment Organism
1.4.99.B3 L-amino acid deaminase
-
 Proteus myxofaciens
1.4.99.B3 LAAD
-
 Proteus myxofaciens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.99.B3 50
-
-
 Proteus myxofaciens

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.4.99.B3 70
-
 negligible activity Proteus myxofaciens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.99.B3 8.5
-
 L-phenylalanine pH 7.5, 25°C Proteus myxofaciens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.99.B3 7 7.5
-
 Proteus myxofaciens

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.4.99.B3 5 9 negligible activity bleow and above Proteus myxofaciens

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.99.B3 FAD an FAD isoalloxazine ring is exposed to solvent Proteus myxofaciens