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TitleCryo-EM structure and rational engineering of a superefficient ochratoxin A-detoxifying amidohydrolase.
Journal, issue, pagesJ Hazard Mater, Vol. 458, Page 131836, Year 2023
Publish dateSep 15, 2023
AuthorsLonghai Dai / Du Niu / Jian-Wen Huang / Xian Li / Panpan Shen / Hao Li / Zhenzhen Xie / Jian Min / Yumei Hu / Yu Yang / Rey-Ting Guo / Chun-Chi Chen /
PubMed AbstractOchratoxin A (OTA) is among the most prevalent mycotoxins detected in agroproducts, posing serious threats to human and livestock health. Using enzymes to conduct OTA detoxification is an appealing ...Ochratoxin A (OTA) is among the most prevalent mycotoxins detected in agroproducts, posing serious threats to human and livestock health. Using enzymes to conduct OTA detoxification is an appealing potential strategy. The recently identified amidohydrolase from Stenotrophomonas acidaminiphila, termed ADH3, is the most efficient OTA-detoxifying enzyme reported thus far and can hydrolyze OTA to nontoxic ochratoxin α (OTα) and L-β-phenylalanine (Phe). To elucidate the catalytic mechanism of ADH3, we solved the single-particle cryo-electron microscopy (cryo-EM) structures of apo-form, Phe- and OTA-bound ADH3 to an overall resolution of 2.5-2.7 Å. The role of OTA-binding residues was investigated by structural, mutagenesis and biochemical analyses. We also rationally engineered ADH3 and obtained variant S88E, whose catalytic activity was elevated by 3.7-fold. Structural analysis of variant S88E indicates that the E88 side chain provides additional hydrogen bond interactions to the OTα moiety. Furthermore, the OTA-hydrolytic activity of variant S88E expressed in Pichia pastoris is comparable to that of Escherichia coli-expressed enzyme, revealing the feasibility of employing the industrial yeast strain to produce ADH3 and its variants for further applications. These results unveil a wealth of information about the catalytic mechanism of ADH3-mediated OTA degradation and provide a blueprint for rational engineering of high-efficiency OTA-detoxifying machineries.
External linksJ Hazard Mater / PubMed:37331057
MethodsEM (single particle)
Resolution2.5 - 2.71 Å
Structure data

EMDB-35452, PDB-8ihq:
Cryo-EM structure of ochratoxin A-detoxifying amidohydrolase ADH3
Method: EM (single particle) / Resolution: 2.71 Å

EMDB-35453, PDB-8ihr:
Cryo-EM structure of ochratoxin A-detoxifying amidohydrolase ADH3 in complex with Phe
Method: EM (single particle) / Resolution: 2.5 Å

EMDB-35454, PDB-8ihs:
Cryo-EM structure of ochratoxin A-detoxifying amidohydrolase ADH3 in complex with ochratoxin A
Method: EM (single particle) / Resolution: 2.5 Å

EMDB-36060, PDB-8j85:
Cryo-EM structure of ochratoxin A-detoxifying amidohydrolase ADH3 mutant S88E in complex with ochratoxin A
Method: EM (single particle) / Resolution: 2.7 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-PHE:
PHENYLALANINE / Phenylalanine

ChemComp-97U:
(2~{S})-2-[[(3~{R})-5-chloranyl-3-methyl-8-oxidanyl-1-oxidanylidene-3,4-dihydroisochromen-7-yl]carbonylamino]-3-phenyl-propanoic acid / toxin*YM / Ochratoxin A

Source
  • stenotrophomonas acidaminiphila (bacteria)
KeywordsHYDROLASE / amidohydrolase / octamer / ochratoxin A degradtion / cryo-EM structure

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