A Novel Enzyme,<scp>L</scp>-Tryptophan Oxidase, from a Basidiomycete,<i>Coprinus</i>sp. SF-1: Purification and Characterization

Furuya, Y.; Sawada, Hidemi; Hirahara, Toshikatsu; Ito, Kazue; Ohshiro, Takashi; Izumi, Yoshikazu

doi:10.1271/bbb.64.1486

Cited by 12 publications

(17 citation statements)

References 16 publications

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“…In Chromobacterium violaceum , the flavoenzyme VioA, an L -amino acid oxidase highly specific for L-TRP, is involved in the synthesis of the purple chromobacterial pigment violacein ( Balibar and Walsh, 2006 ). In the basidiomycete Coprinus , a membrane-bound L -tryptophan oxidase (TOD) catalyzes the simultaneous oxidative deamination and oxidative decarboxylation of L-TRP to produce IPyA and IAM, respectively ( Furuya et al, 2000 ). Therefore, it is possible that LAAO of G. diazotrophicus can catalyze the conversion of L -tryptophan to IPyA, the first step of IAA biosynthesis by IPyA pathway, a role that needs to be further confirmed.…”

Section: Discussionmentioning

confidence: 99%

Identification of Genes Involved in Indole-3-Acetic Acid Biosynthesis by Gluconacetobacter diazotrophicus PAL5 Strain Using Transposon Mutagenesis

et al. 2016

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Gluconacetobacter diazotrophicus is a beneficial nitrogen-fixing endophyte found in association with sugarcane plants and other important crops. Beneficial effects of G. diazotrophicus on sugarcane growth and productivity have been attributed to biological nitrogen fixation process and production of phytohormones especially indole-3-acetic acid (IAA); however, information about the biosynthesis and function of IAA in G. diazotrophicus is still scarce. Therefore, the aim of this work was to identify genes and pathways involved in IAA biosynthesis in this bacterium. In our study, the screening of two independent Tn5 mutant libraries of PAL5T strain using the Salkowski colorimetric assay revealed two mutants (Gdiaa34 and Gdiaa01), which exhibited 95% less indolic compounds than the parental strain when grown in LGIP medium supplemented with L-tryptophan. HPLC chromatograms of the wild-type strain revealed the presence of IAA and of the biosynthetic intermediates indole-3-pyruvic acid (IPyA) and indole-3-lactate (ILA). In contrast, the HPLC profiles of both mutants showed no IAA but only a large peak of non-metabolized tryptophan and low levels of IPyA and ILA were detected. Molecular characterization revealed that Gdiaa01 and Gdiaa34 mutants had unique Tn5 insertions at different sites within the GDI2456 open read frame, which is predicted to encode a L-amino acid oxidase (LAAO). GDI2456 (lao gene) forms a cluster with GDI2455 and GDI2454 ORFs, which are predicted to encode a cytochrome C and an RidA protein, respectively. RT-qPCR showed that transcript levels of lao. cccA, and ridA genes were reduced in the Gdiaa01 as compared to PAL5T. In addition, rice plants inoculated with Gdiaa01 showed significantly smaller root development (length, surface area, number of forks and tips) than those plants inoculated with PAL5T. In conclusion, our study demonstrated that G. diazotrophicus PAL5T produces IAA via the IPyA pathway in cultures supplemented with tryptophan and provides evidence for the involvement of an L-amino acid oxidase gene cluster in the biosynthesis of IAA. Furthermore, we showed that the mutant strains with reduction in IAA biosynthesis ability, in consequence of the lower transcription levels of genes of the lao cluster, had remarkable effects on development of rice roots.

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Section: Discussionmentioning

confidence: 99%

Identification of Genes Involved in Indole-3-Acetic Acid Biosynthesis by Gluconacetobacter diazotrophicus PAL5 Strain Using Transposon Mutagenesis

et al. 2016

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“…While that from Coprinus sp. SF-1 [27] is relatively selective for tryptophan, this LAAO also oxidizes phenylalanine and tyrosine (Table 2). Moreover, this enzyme is not suitable for analyzing samples containing a low concentration of L-tryptophan because of its high Km value of 650 µM.…”

Section: Discussionmentioning

confidence: 99%

“…An enzyme from a basidiomycete, Coprinus sp. SF-1, has been reported to be relatively specific for tryptophan [27]. However, its substrate specificity is insufficient for selective quantification because of its reactivity with phenylalanine and tyrosine.…”

Section: Introductionmentioning

confidence: 99%

Selective tryptophan determination using tryptophan oxidases involved in bis-indole antibiotic biosynthesis

Kameya

Onaka

Asano

2013

Analytical Biochemistry

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A novel tryptophan assay was developed using tryptophan oxidases. Although many l-amino acid oxidases (LAAOs) have been reported to catalyze tryptophan oxidation, most of them have broad substrate specificity and oxidize multiple amino acids besides tryptophan. To obtain a tryptophan-specific LAAO, we focused on bis-indole antibiotic biosynthesis, a bacterial secondary metabolic pathway. A putative LAAO from Streptomyces sp. TP-A0274, StaO involved in staurosporine biosynthesis, was heterologously expressed, biochemically characterized, and shown to serve as a selective tryptophan oxidase for the first time. In addition, another LAAO, VioA involved in violacein biosynthesis in Chromobacterium violaceum, was characterized for comparison with StaO. Interestingly, StaO and VioA share similar properties, namely narrow substrate specificity and high affinity for l-tryptophan, despite the phylogenetic distance between these enzymes. Owing to these features, uncommon among known LAAOs, StaO and VioA assays can be used for selective and accurate quantification of l-tryptophan via a coupled colorimetric reaction. Indeed, StaO and VioA assays provided tryptophan concentrations in human plasma as accurately as those obtained by high-performance liquid chromatography. Therefore, these enzymes were clearly shown to offer an effective method for determining tryptophan in biological samples rapidly, inexpensively, and accurately. The results shown here also suggest the possibility of metabolism-oriented screening as a strategy to obtain enzymes highly selective for individual biomolecules.

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“…SF-1 LAAO catalyzes specifically the oxidative deamination of l -tryptophan, although it can also catalyze its decarboxylation depending on conditions. This oxidase is supposed to be involved in the l -tryptophan metabolism of the fungus [ 78 ].…”

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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A Novel Enzyme,L-Tryptophan Oxidase, from a Basidiomycete,Coprinussp. SF-1: Purification and Characterization

Cited by 12 publications

References 16 publications

Identification of Genes Involved in Indole-3-Acetic Acid Biosynthesis by Gluconacetobacter diazotrophicus PAL5 Strain Using Transposon Mutagenesis

Identification of Genes Involved in Indole-3-Acetic Acid Biosynthesis by Gluconacetobacter diazotrophicus PAL5 Strain Using Transposon Mutagenesis

Selective tryptophan determination using tryptophan oxidases involved in bis-indole antibiotic biosynthesis

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

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