2016
DOI: 10.1074/jbc.m115.703819
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Structure-Function Relationships in l-Amino Acid Deaminase, a Flavoprotein Belonging to a Novel Class of Biotechnologically Relevant Enzymes

Abstract: L-Amino acid deaminase from Proteus myxofaciens (Pma-LAAD) is a membrane flavoenzyme that catalyzes the deamination of neutral and aromatic L-amino acids into ␣-keto acids and ammonia. PmaLAAD does not use dioxygen to re-oxidize reduced FADH 2 and thus does not produce hydrogen peroxide; instead, it uses a cytochrome b-like protein as an electron acceptor. Although the overall fold of this enzyme resembles that of known amine or amino acid oxidases, it shows the following specific structural features: an addit… Show more

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Cited by 54 publications
(71 citation statements)
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“…Overexpressed in E. coli cells, the enzyme was easily purified by a single chromatographic step, recovered full activity when incubated with membranes and, notably, did not require exogeneous FAD for maximal activity. The activity of PmaLAAD is highest at pH 7.5 and at 50 °C; indeed, the enzyme is quite stable . PmaLAAD prefers bulky and hydrophobic substrates, such as l ‐Phe, l ‐Leu, l ‐Met, and l ‐Trp, followed by the polar amino acid l ‐Cys.…”
Section: Introductionmentioning
confidence: 97%
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“…Overexpressed in E. coli cells, the enzyme was easily purified by a single chromatographic step, recovered full activity when incubated with membranes and, notably, did not require exogeneous FAD for maximal activity. The activity of PmaLAAD is highest at pH 7.5 and at 50 °C; indeed, the enzyme is quite stable . PmaLAAD prefers bulky and hydrophobic substrates, such as l ‐Phe, l ‐Leu, l ‐Met, and l ‐Trp, followed by the polar amino acid l ‐Cys.…”
Section: Introductionmentioning
confidence: 97%
“…Here, a suitable alternative is represented by l ‐amino acid deaminase (LAAD). This membrane‐associated, FAD‐containing enzyme catalyzes the O 2 ‐dependent deamination of l ‐amino acids similarly to LAAO (and DAAO on the opposite enantiomer), in this case also yielding the corresponding α‐keto acids and ammonia; however, the electrons are transferred from the reduced cofactor to a cytochrome‐b‐like acceptor without producing any hydrogen peroxide (see Scheme A) …”
Section: Introductionmentioning
confidence: 99%
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