Structural and functional characterization of ochratoxinase, a novel mycotoxin-degrading enzyme
(2014) In Biochemical Journal 462. p.441-452- Abstract
- Ochratoxin, with ochratoxin A as the dominant form, is one of the five major mycotoxins most harmful to humans and animals. It is produced by Aspergillus and Penicillium species and occurs in a wide range of agricultural products. Detoxification of contaminated food is a challenging health issue. In the present paper we report the identification, characterization and crystal structure (at 2.2 angstrom) of a novel microbial ochratoxinase from Aspergillus niger. A putative amidase gene encoding a 480 amino acid polypeptide was cloned and homologously expressed in A. niger. The recombinant protein is N-terminally truncated, thermostable, has optimal activity at pH similar to 6 and 66 degrees C, and is more efficient in ochratoxin A hydrolysis... (More)
- Ochratoxin, with ochratoxin A as the dominant form, is one of the five major mycotoxins most harmful to humans and animals. It is produced by Aspergillus and Penicillium species and occurs in a wide range of agricultural products. Detoxification of contaminated food is a challenging health issue. In the present paper we report the identification, characterization and crystal structure (at 2.2 angstrom) of a novel microbial ochratoxinase from Aspergillus niger. A putative amidase gene encoding a 480 amino acid polypeptide was cloned and homologously expressed in A. niger. The recombinant protein is N-terminally truncated, thermostable, has optimal activity at pH similar to 6 and 66 degrees C, and is more efficient in ochratoxin A hydrolysis than carboxypeptidase A and Y, the two previously known enzymes capable of degrading this mycotoxin. The subunit of the homo-octameric enzyme folds into a two-domain structure characteristic of a metal dependent amidohydrolase, with a twisted TIM (triosephosphateisomerase)-barrel and a smaller beta-sandwich domain. The active site contains an aspartate residue for acid base catalysis, and a carboxylated lysine and four histidine residues for binding of a binuclear metal centre. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4702685
- author
- Dobritzsch, Doreen ; Wang, Huaming ; Schneider, Gunter and Yu, Shukun LU
- organization
- publishing date
- 2014
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- metal-dependent amidohydrolase, mycotoxin, ochratoxin degradation, protein crystal structure
- in
- Biochemical Journal
- volume
- 462
- pages
- 441 - 452
- publisher
- Portland Press
- external identifiers
-
- wos:000341802100006
- scopus:84907311620
- pmid:24947135
- ISSN
- 0264-6021
- DOI
- 10.1042/BJ20140382
- language
- English
- LU publication?
- yes
- id
- c761aeac-b34e-4565-9ad5-5010ac23f901 (old id 4702685)
- date added to LUP
- 2016-04-01 13:45:57
- date last changed
- 2025-10-14 13:00:38
@article{c761aeac-b34e-4565-9ad5-5010ac23f901,
abstract = {{Ochratoxin, with ochratoxin A as the dominant form, is one of the five major mycotoxins most harmful to humans and animals. It is produced by Aspergillus and Penicillium species and occurs in a wide range of agricultural products. Detoxification of contaminated food is a challenging health issue. In the present paper we report the identification, characterization and crystal structure (at 2.2 angstrom) of a novel microbial ochratoxinase from Aspergillus niger. A putative amidase gene encoding a 480 amino acid polypeptide was cloned and homologously expressed in A. niger. The recombinant protein is N-terminally truncated, thermostable, has optimal activity at pH similar to 6 and 66 degrees C, and is more efficient in ochratoxin A hydrolysis than carboxypeptidase A and Y, the two previously known enzymes capable of degrading this mycotoxin. The subunit of the homo-octameric enzyme folds into a two-domain structure characteristic of a metal dependent amidohydrolase, with a twisted TIM (triosephosphateisomerase)-barrel and a smaller beta-sandwich domain. The active site contains an aspartate residue for acid base catalysis, and a carboxylated lysine and four histidine residues for binding of a binuclear metal centre.}},
author = {{Dobritzsch, Doreen and Wang, Huaming and Schneider, Gunter and Yu, Shukun}},
issn = {{0264-6021}},
keywords = {{metal-dependent amidohydrolase; mycotoxin; ochratoxin degradation; protein crystal structure}},
language = {{eng}},
pages = {{441--452}},
publisher = {{Portland Press}},
series = {{Biochemical Journal}},
title = {{Structural and functional characterization of ochratoxinase, a novel mycotoxin-degrading enzyme}},
url = {{http://dx.doi.org/10.1042/BJ20140382}},
doi = {{10.1042/BJ20140382}},
volume = {{462}},
year = {{2014}},
}