Sökning: onr:"swepub:oai:DiVA.org:uu-235169" >
Structural and func...
Structural and functional characterization of ochratoxinase, a novel mycotoxin-degrading enzyme
-
- Dobritzsch, Doreen, 1972- (författare)
- Uppsala universitet,Biokemi,Dobritzsch
-
Wang, Huaming (författare)
-
- Schneider, Gunter (författare)
- Karolinska Institutet
-
visa fler...
-
- Yu, Shukun (författare)
- Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
-
visa färre...
-
(creator_code:org_t)
- 2014
- 2014
- Engelska.
-
Ingår i: Biochemical Journal. - 0264-6021 .- 1470-8728. ; 462:3, s. 441-452
- Relaterad länk:
-
http://dx.doi.org/10...
-
visa fler...
-
https://urn.kb.se/re...
-
https://doi.org/10.1...
-
https://lup.lub.lu.s...
-
http://kipublication...
-
visa färre...
Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- metal-dependent amidohydrolase
- mycotoxin
- ochratoxin degradation
- protein crystal structure
- metal-dependent amidohydrolase
- mycotoxin
- ochratoxin degradation
- protein crystal structure
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas