1.4.99.B3: L-amino acid dehydrogenase (cytochrome b)

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For detailed information about L-amino acid dehydrogenase (cytochrome b), go to the full flat file.

Word Map on EC 1.4.99.B3

1.4.99.B3

proteus

mirabilis

vulgaris

l-phenylalanine

deamination

biocatalysis

ppa

phenylpyruvic

d-amino

l-leucine

d-lactate

enantiomerically

fadh2

flavoenzyme

Reaction

+ 2 cytochrome b =

+ 2 reduced cytochrome b

Synonyms

L-amino acid deaminase, LAAD

ECTree

1 Oxidoreductases

1.4 Acting on the CH-NH₂ group of donors

1.4.99 With unknown physiological acceptors

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

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Results	in table
1	AA Sequence
2	Cloned(Commentary)
1	Cofactor
1	Crystallization (Commentary)
1	General Stability
1	Inhibitors
2	KM Value [mM]
2	Localization
3	Molecular Weight [Da]
4	Organism
3	pH Optimum
1	pH Range
1	Protein Variants
1	Reaction
4	Reference
1	Specific Activity [micromol/min/mg]
2	Storage Stability
33	Substrates and Products (Substrate)
3	Subunits
2	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
1	Temperature Range [°C]
1	Turnover Number [1/s]

Crystallization

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

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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

A0A158RFS7

740746