Purification and characterization of monoamine oxidase from Klebsiella aerogenes

Yamashita, Mitsuo; Sakaue, Masashi; Iwata, Nobuhide; Sugino, Hiroyuki; Murooka, Yoshikatsu

doi:10.1016/0922-338x(93)90196-f

Cited by 40 publications

(29 citation statements)

References 42 publications

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“…Elucidation of the 1,4-diamin0-2-butynebinding site and its consensus sequence is now in progress. When the amino acid sequence near the active site, towards, the amino terminus, was compared for amine oxidases from various sources [23,[26][27][28][29][30][31][32], as shown in Fig. 9, some similarity around the position of the 1,4-diamino-2-butyne-binding site of A. niger AO-I was found.…”

Section: 4 1 E T I a D Y T G K P T T I P G A V A I F E R Y A G P E mentioning

confidence: 99%

“…9, some similarity around the position of the 1,4-diamino-2-butyne-binding site of A. niger AO-I was found. But only bovine plasma amine oxidase [31] contains a lysyl residue in the same position as A. niger AO-I, although amine oxidases from Hansenula polymorpha [28] and Klebsiella aerogenes [30] also contain lysyl residues close to this position.…”

Section: 4 1 E T I a D Y T G K P T T I P G A V A I F E R Y A G P E mentioning

confidence: 99%

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Active‐Site Covalent Modifications of Quinoprotein Amine Oxidases from Aspergillus niger

Frébort¹,

Peč

Luhová

et al. 1994

European Journal of Biochemistry

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Interactions of two distinct quinoprotein amine oxidases from Aspergillus niger, AO-I and AO-11, with active-site covalent modifiers have been investigated. Both enzymes are inhibited similarly by phenylhydrazine or p-nitrophenylhydrazine, forming an orange Schiff base with a carbonyl group of topaquinone cofactor. Modification of histidyl and tyrosyl residues by diethylpyrocarbonate and sulfhydryl groups by 5,5'-dithio-bis-(2-nitrobenzoic acid) and 4-chloro-7-nitrobenzo-2-oxa-l,3-diazole have been described. A substrate analog, 1,4-diamino-2-butyne, was found to function as a mechanism-based inhibitor. It shows both substrate saturation kinetics and time-dependent irreversible inhibition caused by formation of pynole bound to the active site. The pyrrole formation was confirmed spectrophotometrically by reaction with Ehrlich's reagent at 525 nm. Inhibition by 1,4-diamino-2-butyne produces a new maximum in the absorption spectra of AO-I and AO-I1 at 310 nm and 306 nm, respectively. Inactivated AO-I was digested by proteases ; labeled peptides were purified by C18 HPLC and sequenced by Edman degradation. Data reveal the evidence that 1P-diamino-2-butyne reacts with the &-amino group of the Lys356 residue in the sequence Lys-Met-Pro-AsnAla of Aspergillus niger amine oxidase AO-I.Amine oxidase of Aspergillus niger is a copper-carbonyl enzyme, which was found in the mid 1960s, purified and crystallized [l, 21. Copper and an undetermined carbonyl cofactor were found to function in the catalytic cycle [2-41. Nowadays, the importance of the fungal amine oxidase has risen again because the enzyme can be applied to monitor histamine contents in fishery products [5]. A massive production of the enzyme on the industrial scale has increased current interest.Recently, we have found two amine oxidases (EC 1.4.3.6), named AO-I and AO-11, in Aspergillus niger mycelia grown on n-butylamine medium [6, 71. AO-I is the enzyme previously reported, consisting of two 75-kDa subunits, while AO-I1 is a novel enzyme of 80 kDa. These amine oxidases do not show big differences in their peptide maps, but differ in their N-terminals. They also do not show any remarkable difference in substrate specificity or sensitivity to inhibitors. The cofactors of both enzymes give a typical reaction with p-nitrophenylhydrazine [6, 71 like other topaquiCorrespondence to I. Frkbort, Laboratory of Applied Microbiology, Faculty of Agriculture, Yarnaguchi University, 1 677-1 Yoshida, Yamaguchi, Japan 753Abbreviations. AO-I and AO-11, Aspergillus niger amine oxidases ; Nbs,, 5,5'-dithio-bis-(2-nitrobenzoic acid) ; buffer A, 0.01 M potassium phosphate pH 7.0.Enzymes. Amine oxidase, arnine:O, oxidoreductase (dearninating) (copper containing) (EC 1.4.3.6) ; peroxidase from horseradish (EC 1.11.1.7); pronase P from Streptomyces griseus (EC 3.4.24.31); thermolysin from Bacillus themolyticus rokko (EC 3.4.24.27 It is very probable that AO-I was purified and crystallized in earlier studies but fractions containing AO-I1 were not purified further because of its lower...

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Section: 4 1 E T I a D Y T G K P T T I P G A V A I F E R Y A G P E mentioning

confidence: 99%

Section: 4 1 E T I a D Y T G K P T T I P G A V A I F E R Y A G P E mentioning

confidence: 99%

Active‐Site Covalent Modifications of Quinoprotein Amine Oxidases from Aspergillus niger

Frébort¹,

Peč

Luhová

et al. 1994

European Journal of Biochemistry

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“…MaoA was overproduced in periplasmic space. The purification, some characterization, and crystallization of MaoA from E. coli have been reported (39,40), the characterization of MaoA from E. coli being almost the same as that from K. aerogenes (39,57).…”

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confidence: 99%

“…This cloning resulted in a high level of production of the soluble form of tyramine oxidase (47), making possible the purification and characterization of tyramine oxidase (57). The enzyme is highly specific for tyramine, ␤-phenylethylamine, and dopamine and contains copper and topa quinone as a prosthetic group (8,57). We classified this enzyme from K. aerogenes as a monoamine oxidase instead of a tyramine oxidase, and hence, the gene encoding this enzyme was renamed maoA instead of tynA (47).…”

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confidence: 99%

maoB, a gene that encodes a positive regulator of the monoamine oxidase gene (maoA) in Escherichia coli

et al. 1996

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The structural gene for copper-and topa quinone-containing monoamine oxidase (maoA) and an unknown amine oxidase gene have been located at 30.9 min on the Escherichia coli chromosome. Deletion analysis showed that the unknown gene was located within a 1.1-kb cloned fragment adjacent to the maoA gene. The nucleotide sequence of this fragment was determined, and a single open reading frame (maoB) consisting of 903 bp was found. The gene encoded a polypeptide with a predicted molecular mass of 34,619 Da which was correlated with the migration on a sodium dodecyl sulfate-polyacrylamide gel. The predicted amino acid sequence of the MaoB protein was identical to the NH 2 -terminal amino acid sequence derived by Edman degradation of the protein synthesized under the self-promoter. No homology of the nucleotide sequence of maoB to the sequences of any reported genes was found. However, the amino acid sequence of MaoB showed a high level of homology with respect to the helix-turn-helix motif of the AraC family in its C terminus. The homology search and disruption of maoA on the chromosome led to the conclusion that MaoB is a transcriptional activator of maoA but not an amine oxidase. The consensus sequence of the cyclic AMP-cyclic AMP receptor protein complex binding domain was adjacent to the putative promoter for the maoB gene. By use of lac gene fusions with the maoA and maoB genes, we showed that the maoA gene is regulated by tyramine and MaoB and that the expression of the maoB gene is subject to catabolite repression. Thus, it seems likely that tyramine and the MaoB protein activate the transcription of maoA by binding to the regulatory region of the maoA gene.

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“…Biogenic amines are physiologically degraded through oxidative deamination catalysed by amines oxidase by the following reaction: R-CH 2 -NH-R' + O 2 + H 2 O → R-CHO + H 2 N-R' + H 2 O 2 (Murooka et al 1979;Ishizuka et al 1993;Yamashita et al 1993). Monoamine and diamine oxidases are ubiquitous and play an important role in the metabolism of amines in human, plant, and animal cells.…”

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confidence: 99%

Occurrence of biogenic amines and amines degrading bacteria in fish sauce

Zaman¹,

Bakar²,

Selamat³

et al. 2010

Czech J. Food Sci.

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Zaman M.Z., Bakar F.A., Selamat J., Bakar J.. (2010): Occurrence of biogenic amines and amines degrading bacteria in fish sauce. Czech J. Food Sci., 28: 440-449.The contents of biogenic amines histamine, putrescine, and cadaverine in fish sauce were determined and the bacteria isolated from the samples were evaluated for their amines degradation activity. Five fish sauce samples contained 62.5-393.3 ppm of histamine, 5.6-242.8 ppm of putrescine, and 187.1-704.7 ppm of cadaverine. Thirty three bacterial isolates produced all three amines, seven isolates produced one or two amines, and one isolate did not produce any amine in differential agar media. Since the strains that produced amines were not supposed to degrade them, only eight isolates were further identified and evaluated for their amines degrading capability. Bacillus amyloliquefaciens FS-05 and Staphylococcus carnosus FS-19 degraded histamine up to 59.9% and 29.1% from its initial concentration, respectively. Staphylococcus intermedius FS-20 and Bacillus subtilis FS-12 degraded putrescine and cadaverine up to 30.4% and 28.9%, respectively. Most isolates tolerated the salt concentration of up to 15% and temperature of up to 45°C. The current study provided new information on biogenic amines degrading bacteria, isolated from high-salt-content food products. The amines degradation activity of the bacteria is considered as strain rather than species specific.

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Purification and characterization of monoamine oxidase from Klebsiella aerogenes

Cited by 40 publications

References 42 publications

Active‐Site Covalent Modifications of Quinoprotein Amine Oxidases from Aspergillus niger

Active‐Site Covalent Modifications of Quinoprotein Amine Oxidases from Aspergillus niger

maoB, a gene that encodes a positive regulator of the monoamine oxidase gene (maoA) in Escherichia coli

Occurrence of biogenic amines and amines degrading bacteria in fish sauce

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