N-acetyl-6-hydroxytryptophan a natural substrate of a monophenol oxidase from Aspergillus nidulans

McCorkindale, N.J.; Hayes, Douglas G.; Johnston, Grant; Clutterbuck, A. J.

doi:10.1016/0031-9422(83)85048-1

Cited by 15 publications

(10 citation statements)

References 4 publications

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“…FscG similarly shows high homology to DMATs. Associated with these are FscE with homology to IvoC, a N-acetyltryptophan 6-hydroxylase, 27 and FscH homologous to kynurenine formidase which deformylates N-formyl-kynurenine to kynurenine. 28 The biosynthesis of fusarochromene would require the epimerization of L-tryptophan 16 to D-tryptophan 17 and consistent with that is the presence of FscC.…”

Section: Papermentioning

confidence: 99%

Fusarochromene, a novel tryptophan-derived metabolite from Fusarium sacchari

et al. 2021

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Section: Papermentioning

confidence: 99%

Fusarochromene, a novel tryptophan-derived metabolite from Fusarium sacchari

et al. 2021

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“…1991), inpB (Bergmann et al ., 2010; Yeh et al ., 2016), sidD (Grundlinger et al . 2013), atnA (Chiang et al ., 2016; Henke et al ., 2016), asqK (Ishikawa et al ., 2014), and ivoA (Mccorkindale et al . 1983; Birse and Clutterbuck 1990) (Table 1).…”

Section: Introductionmentioning

confidence: 99%

Overexpression of a three-gene conidial pigment biosynthetic pathway in Aspergillus nidulans reveals the first NRPS known to acetylate tryptophan

Sung

Chang

Entwistle

et al. 2017

Fungal Genetics and Biology

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Fungal nonribosomal peptide synthetases (NRPSs) are megasynthetases that produce cyclic and acyclic peptides. In Aspergillus nidulans, the NRPS ivoA (AN10576) has been associated with the biosynthesis of grey-brown conidiophore pigments. Another gene, ivoB (AN0231), has been demonstrated to be an N-acetyl-6-hydroxytryptophan oxidase that putatively acts downstream of IvoA. A third gene, ivoC, has also been predicted to be involved in pigment biosynthesis based on publicly available genomic and transcriptomic information. In this paper, we report the replacement of the promoters of the ivoA, ivoB, and ivoC genes with the inducible promoter alcA in a single cotransformation. Co-overexpression of the three genes resulted in the production of a dark-brown pigment in hyphae. In addition, overexpression of each of the Ivo genes, ivoA-C, individually or in combination, allowed us to isolate intermediates and confirm the function of each gene. IvoA was found to be the first known NRPS to carry out the acetylation of the amino acid, tryptophan.

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“…Purified AHT extracted from ivoB strains has been compared with the synthetic product (McCorkindale et al, 1983). Both are substrates for the phenol oxidase as assayed polarographically and by destruction of substrate as determined with diazotized sulphanilic acid.…”

Section: 4mentioning

confidence: 99%

“…The natural substrate is accumulated by ivoB mutants, which lack the phenol oxidase described in this paper (Clutterbuck, 1990). It has been purified in small quantities (McCorkindale et al, 1983) and shown to be N-acetyl-6-hydroxytryptophan (AHT: Fig. 1 a).…”

Section: 4mentioning

confidence: 99%

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N-Acetyl-6-hydroxytryptophan oxidase, a developmentally controlled phenol oxidase from Aspergillus nidulans

Birse

Clutterbuck

1990

Journal of General Microbiology

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We have purified a specific phenol oxidase which is produced during conidiophore development in the fungus AspergiZZus niduZms. Two active forms (A and B) have molecular masses of 50 and 48 kDa respectively; they have identical N-termini (24 residues). We have analysed the metal ion content of the B form; it is unusual in consisting of one zinc and two copper atoms per molecule. A temperature-sensitive mutant (ivoB192) produces a thermolabile enzyme, implying that ivoB is the structural locus. The natural substrate of the enzyme is N-acetyl-6-hydroxytryptophan, but it can be assayed colorimetrically or polarographically using hydroquinone monomethyl ether (HME) as substrate. It will also oxidize p-cresol, but not tyrosine, 3,4-dihydroxyphenylalanine or o-methoxyphenol. Colour development with HME substrate is strongly enhanced by high ammonium ion concentrations. Activity against HME is inhibited by 2,3-dihydroxynaphthalene, phenylhydrazine, diethyl dithiocarbamate and &hydroxyquinolene.

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N-acetyl-6-hydroxytryptophan a natural substrate of a monophenol oxidase from Aspergillus nidulans

Cited by 15 publications

References 4 publications

Fusarochromene, a novel tryptophan-derived metabolite from Fusarium sacchari

Fusarochromene, a novel tryptophan-derived metabolite from Fusarium sacchari

Overexpression of a three-gene conidial pigment biosynthetic pathway in Aspergillus nidulans reveals the first NRPS known to acetylate tryptophan

N-Acetyl-6-hydroxytryptophan oxidase, a developmentally controlled phenol oxidase from Aspergillus nidulans

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