Enzymatic determination of l-lysine by flow-injection techniques

Pohlmann, Andreas; Stamm, Wolfgang W.; Kusakabe, Hitoshi; Kula, Maria‐Regina

doi:10.1016/s0003-2670(00)82091-7

Cited by 35 publications

(7 citation statements)

References 30 publications

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“…LysOX is expected to be a potential anti-cancer agent since it inhibits growth of cancer cells but shows relatively low cytotoxicity for normal cells [ 72 , 73 ]. Furthermore, LysOX is stable over a wide range of pH and temperature, so it is an attractive candidate for an enzyme-based l -lysine sensor [ 74 , 75 ]. More recently, an extracellular LAAO with antimicrobial activity has been isolated from Trichoderma harzianum ETS 323.…”

Section: Phylogenetic Analysis Of Proteins With Amino Acid Oxidasementioning

confidence: 99%

Distribution in Different Organisms of Amino Acid Oxidases with FAD or a Quinone As Cofactor and Their Role as Antimicrobial Proteins in Marine Bacteria

2015

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Amino acid oxidases (AAOs) catalyze the oxidative deamination of amino acids releasing ammonium and hydrogen peroxide. Several kinds of these enzymes have been reported. Depending on the amino acid isomer used as a substrate, it is possible to differentiate between l-amino acid oxidases and d-amino acid oxidases. Both use FAD as cofactor and oxidize the amino acid in the alpha position releasing the corresponding keto acid. Recently, a novel class of AAOs has been described that does not contain FAD as cofactor, but a quinone generated by post-translational modification of residues in the same protein. These proteins are named as LodA-like proteins, after the first member of this group described, LodA, a lysine epsilon oxidase synthesized by the marine bacterium Marinomonas mediterranea. In this review, a phylogenetic analysis of all the enzymes described with AAO activity has been performed. It is shown that it is possible to recognize different groups of these enzymes and those containing the quinone cofactor are clearly differentiated. In marine bacteria, particularly in the genus Pseudoalteromonas, most of the proteins described as antimicrobial because of their capacity to generate hydrogen peroxide belong to the group of LodA-like proteins.

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Section: Phylogenetic Analysis Of Proteins With Amino Acid Oxidasementioning

confidence: 99%

Distribution in Different Organisms of Amino Acid Oxidases with FAD or a Quinone As Cofactor and Their Role as Antimicrobial Proteins in Marine Bacteria

2015

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“…Thus, LysOX from T. viride is a potential candidate for an enzyme-based amino acid sensor. 9 The crystal structure of LysOX without substrate revealed that LysOX is composed of three domains, the FAD-binding domain, the substrate-binding domain, and the helical domain, like snake venom LAAOs. 8 Comparison of the substrate-binding site of LysOX with those of other known LAAOs [10][11][12][13][14][15] revealed that the residues involved in recognition of the L-amino acid backbone are structurally conserved although the amino acid sequence identity to the snake LAAOs is only around 20%, suggesting that oxidative deamination reaction of LysOX proceeds in the same manner as other LAAOs.…”

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confidence: 99%

Structural basis of strict substrate recognition of l‐lysine α‐oxidase from Trichoderma viride

et al. 2020

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L-Lysine oxidase (LysOX) is a FAD-dependent homodimeric enzyme that catalyzes the oxidative deamination of L-lysine to produce α-keto-ε-aminocaproate with ammonia and hydrogen peroxide. LysOX shows strict substrate specificity for L-lysine, whereas most L-amino acid oxidases (LAAOs) exhibit broad substrate specificity for L-amino acids. Previous studies of LysOX showed that overall structural similarity to the well-studied snake venom LAAOs. However, the molecular mechanism of strict specificity for L-lysine was still unclear. We here determined the structure of LysOX in complex with L-lysine at 1.7 Å resolution. The structure revealed that the hydrogen bonding network formed by D212, D315, and A440 with two water molecules is responsible for the recognition of the side chain amino group. In addition, a narrow hole formed by five hydrophobic residues in the active site contributes to strict substrate specificity. Mutation studies demonstrated that D212 and D315 are essential for L-lysine recognition, and the D212A/D315A double mutant LysOX showed different substrate specificity from LysOX. Moreover, the structural basis of the substrate specificity change has also been revealed by the structural analysis of the mutant variant and its substrate complexes. These results clearly explain the molecular mechanism of the strict specificity of LysOX and suggest that LysOX is a potential candidate for a template to design LAAOs specific to other L-amino acids.

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“…Considerable studies have been devoted to azo dyes derived from 4-aminoantipyrine [15][16][17][18][19]. Fadda et al [20][21][22][23][24], have been reported the synthesis of different azo disperse dyes for synthetic fibres.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of Novel Azo Disperse dyes Derived from 4-Aminoantipyrine and their Applications to Polyester Fabrics

Fadda¹,

Elattar²

2012

AJOC

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Nine variously substituted azo dyes derivatives 2-10 of antipyrine were prepared. The effects of the nature and orientation of the substituents on the color and dyeing properties of these dyes on polyester fibres were evaluated. The newly synthesized compounds were characterized by elemental analyses and spectral data (IR, 1 H NMR, 13 C-NMR and MS). The investigated dyes were applied t o polyester f a b r i c s and showed good light, washing, heat and acid perspiration fastness. The remarkable degree of brightness after washings is indicative of good penetration and the excellent affinity of these dyes for the fabric. The results in general revealed the efficiency of the prepared compounds as new azo dyes.

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Enzymatic determination of l-lysine by flow-injection techniques

Cited by 35 publications

References 30 publications

Distribution in Different Organisms of Amino Acid Oxidases with FAD or a Quinone As Cofactor and Their Role as Antimicrobial Proteins in Marine Bacteria

Distribution in Different Organisms of Amino Acid Oxidases with FAD or a Quinone As Cofactor and Their Role as Antimicrobial Proteins in Marine Bacteria

Structural basis of strict substrate recognition of l‐lysine α‐oxidase from Trichoderma viride

Synthesis of Novel Azo Disperse dyes Derived from 4-Aminoantipyrine and their Applications to Polyester Fabrics

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