Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion‐dependent autooxidation of a specific tyrosyl residue

Matsuzaki, Ryuichi; Fukui, Tsuguya; Sato, Hidetoshi; Ozaki, Yukihiro; Tanizawa, Katsuyuki

doi:10.1016/0014-5793(94)00884-1

Cited by 184 publications

(216 citation statements)

References 17 publications

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“…Arnow's test is shown to be specific for o-substituted dihydroxyphenols. This confirms the presence of a Dopa residue in blue PMI, and suggests that the modified residue in blue PMI is not trihydroxyphenylalanine quinone (Topa quinone) which can be autocatalytically generated in the active site of copper amine oxidases by cupric ions (Matsuzaki et al, 1994).…”

Section: Discussionsupporting

confidence: 53%

Identification of an Fe(III)‐dihydroxyphenylalanine Site in Recombinant Phosphomannose Isomerase from Candida albicans

Smith¹,

Thomson²,

Proudfoot³

et al. 1997

European Journal of Biochemistry

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Candida albicans phosphomannose isomerase (PMI) is a zinc metalloprotein of known crystal structure. When heterologously overexpressed in Escherichia coli, a blue protein that contains up to 0.5 iron atoms/PMI molecule could be isolated, with absorption maxima at 420 nm and 680 nm. These bands are reminiscent of ferric catecholate complexes, an assignment that has been confirmed by resonance Raman spectroscopy, and by reaction with Arnow's reagent, which is specific for the presence of 3,4-dihydroxyphenylalanine (Dopa). After enzymatic digestion of blue PMI, a peptide with the sequence DPHAXISG was isolated corresponding to residues Asp283 -Gly290 in the amino acid sequence of C. albicans PMI, where the unidentified residue X287 is encoded by a tyrosine codon. It is proposed that iron and oxygen bring about hydroxylation of Tyr287 in PMI and that Fe(II1) subsequently chelates the Dopa residue to give the characteristic absorption spectrum. The EPR spectrum of the blue protein suggests three iron environments in the protein, two in axial environments with EID values approximately equal to 0.06 and 0.12 and one rhombic species. The nature of the iron co-ordination sites is discussed with the help of model systems and by comparison with other blue non-heme iron proteins.Keywords: phosphomannose isomerase; Fe(II1)-dopamine complex ; zinc-dependent metalloenzyme ; EPR.Phosphomannose isomerase (PMI) catalyses the interconversion of fructose 6-phosphate and mannose 6-phosphate. The enzyme originally isolated from baker's yeast was shown to be a monomeric protein of molecular mass 45 kDa. It contains one zinc atodprotein monomer (Gracy and Noltmann, 1968 a). The enzyme catalyses the first committed step in the synthesis of cell wall mannoproteins from glycolytic intermediates. Temperaturesensitive mutations in the gene for PMI cause cell lysis and death at the restrictive temperature in both Saccharomyces cerevisiae (Smith et al., 1992) and Candida albicans (Smith et al., 1995). PMI is therefore a suitable target for the development of an inhibitory antifungal agent.The gene coding for PMI has been recently cloned from an ordered array genomic library of C. albicans cDNA (Smith et al., 1995) and overexpressed in Escherichia coli. Metal analysis of the recombinant protein showed the presence of almost one zinc ionIprotein monomer (Wells, T. N. C., unpublished results). However, at very high concentrations, for example greater than 50 mg/ml used in setting up crystallisation experiments (Tolley et al., 1994), the protein appeared blue. Comparison of the ultraviolet-visible range absorption spectrum with that of tyrosine hydroxylase Enzyme. Mannose-6-phosphate isomerase (phosphomannose isomerase) (EC 5.3.1.8).ion analysis showed the presence of 0.2 iron atomsIprotein molecule.Fermentation of E. coli under higher concentrations (1 mM) of FeSO, leads to the formation of a blue protein with a maximal iron concentration of 0.5 iron atomdprotein molecule. We have therefore analysed the protein and shown the blue colour to be ...

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Section: Discussionsupporting

confidence: 53%

Identification of an Fe(III)‐dihydroxyphenylalanine Site in Recombinant Phosphomannose Isomerase from Candida albicans

Smith¹,

Thomson²,

Proudfoot³

et al. 1997

European Journal of Biochemistry

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“…The amine oxidase is of particular interest because it is a member of the copper-topaquinone family of amine oxidases (Cooper et al, 1992) whose organic co-factor is formed autocatalytically (Matsuzaki et al, 1994;Hanlon et al, 1995). Recently, a second amine oxidase gene was reported to be located very close to the gene encoding the 2-phenylethylamine oxidase (PEO) (Azakami et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

2-Phenylethylamine catabolism by Escherichia coli K-12: gene organization and expression

et al. 1997

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“…A more than 40 % inhibition was found for aminoguanidine, 1-amino-3-phenyl-3-propanone, 1,5-diamino-3-pentanone, benzaldehyde oxime, phenylhydrazine, and benzo-phenanthridine alkaloids, chelerythrine and fagaronine. 3. pH dependence of specific activity of GFAO with substrates: n-butylamine (I), nhexylamine (O), benzylamine (Q) and histamine (O).…”

Section: Substrates and Inhibitorsmentioning

confidence: 99%

“…Copper ion and an organic cofactor topaquinone [2], which is formed by autooxidation of a specific tyrosyl residue [3], mediate the catalytic reaction proceeding by a pingpong mechanism with Cu(I)-semiquinone as an intermediate [4]. A complete amino acid sequence has become available for several amine oxidases [5] and recently the crystal structure of the amine oxidase from Escherichia coli has been determined in both active and inactive forms [6].…”

Section: Introductionmentioning

confidence: 99%

The fungus Gibberella fujikuroi produces copper/topaquinone‐containing amine oxidase when induced by n‐butylamine

1997

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SUMMARYCrude extract of Gibberellafujikuroi AKU 3802 mycelium induced with n-butylamine showed a single amine oxidase activity band in a non-denaturing gel that cross-reacted with the antibody against copper/topaquinone-containing amine oxidase from AspergiUus niger. The enzyme was purified by a procedure involving four chromatographic steps. Purified enzyme was pink with an absorption maximum at 490 nm. Molecular mass of 135 kDa estimated by gel chromatography and 70 kDa found by SDS-PAGE confirmed the dimeric structure of the enzyme. The enzyme readily oxidized n-hexylamine, n-butylamine, benzylamine and histamine, but not spermine or spermidine. Inactivation by carbonyl reagents and copper chelators suggested the presence of a copper/topaquinone cofactor. Spectrophotometric titration by p-nitrophenylhydrazine showed one reactive carbonyl group per subunit and redox-cyclic quinone staining confirmed the presence of a quinone cofactor, pH-dependent shift of the absorption spectrum of the enzyme pnitrophenylhydrazone (465 nm at neutral to 580 nm at alkaline pH) supports the identity of the cofactor with topaquinone. The N-terminal amino acid sequence of the enzyme showed high similarity to other microbial copper/topaquinone-containing amine oxidases.

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Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion‐dependent autooxidation of a specific tyrosyl residue

Cited by 184 publications

References 17 publications

Identification of an Fe(III)‐dihydroxyphenylalanine Site in Recombinant Phosphomannose Isomerase from Candida albicans

Identification of an Fe(III)‐dihydroxyphenylalanine Site in Recombinant Phosphomannose Isomerase from Candida albicans

2-Phenylethylamine catabolism by Escherichia coli K-12: gene organization and expression

The fungus Gibberella fujikuroi produces copper/topaquinone‐containing amine oxidase when induced by n‐butylamine

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