Bacterial Lactonases ZenA with Noncanonical Structural Features
Hydrolyze the Mycotoxin Zearalenone

J 2024

Bacterial Lactonases ZenA with Noncanonical Structural Features Hydrolyze the Mycotoxin Zearalenone

FRUHAUF, Sebastian; Dominic PUHRINGER; Michaela THAMHESL; Patricia FAJTL; Elisavet KUNZ-VEKIRU et al.

Základní údaje

Originální název

Bacterial Lactonases ZenA with Noncanonical Structural Features Hydrolyze the Mycotoxin Zearalenone

Autoři

Vydání

ACS Catalysis, WASHINGTON, AMER CHEMICAL SOC, 2024, 2155-5435

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10403 Physical chemistry

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 13.100

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/24:00135625

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

zearalenone; mycotoxin; lactonase; carboxylesterase; hydrolase; kinetics; presteady-state; Rhodococcus erythropolis

Štítky

14314010, 143180, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 24. 2. 2025 09:11, Mgr. Michaela Hylsová, Ph.D.

Anotace

V originále

Zearalenone (ZEN) is a mycoestrogenic polyketide produced by Fusarium graminearum and other phytopathogenic members of the genus Fusarium. Contamination of cereals with ZEN is frequent, and hydrolytic detoxification with fungal lactonases has been explored. Here, we report the isolation of a bacterial strain, Rhodococcus erythropolis PFA D8-1, with ZEN hydrolyzing activity, cloning of the gene encoding alpha/beta hydrolase ZenA encoded on the linear megaplasmid pSFRL1, and biochemical characterization of nine homologues. Furthermore, we report site-directed mutagenesis as well as structural analysis of the dimeric ZenA(Re) of R. erythropolis and the more thermostable, tetrameric ZenA(Scfl) of Streptomyces coelicoflavus with and without bound ligands. The X-ray crystal structures not only revealed canonical features of alpha/beta hydrolases with a cap domain including a Ser-His-Asp catalytic triad but also unusual features including an uncommon oxyanion hole motif and a peripheral, short antiparallel beta-sheet involved in tetramer interactions. Presteady-state kinetic analyses for ZenA(Re) and ZenA(Scfl) identified balanced rate-limiting steps of the reaction cycle, which can change depending on temperature. Some new bacterial ZEN lactonases have lower K-M and higher k(cat) than the known fungal ZEN lactonases and may lend themselves to enzyme technology development for the degradation of ZEN in feed or food.

Návaznosti

EF17_043/0009632, projekt VaV

Název: CETOCOEN Excellence

LM2023055, projekt VaV

Název: Česká národní infrastruktura pro biologická data

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, ELIXIR-CZ: Česká národní infrastruktura pro biologická data

LX22NPO5107, projekt VaV

Název: Národní ústav pro neurologický výzkum

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Národní ústav pro neurologický výzkum, 5.1 EXCELES

857560, interní kód MU
(Kód CEP: EF17_043/0009632)

Název: CETOCOEN Excellence (Akronym: CETOCOEN Excellence)

Investor: Evropská unie, CETOCOEN Excellence, Spreading excellence and widening participation

90269, velká výzkumná infrastruktura

Název: RECETOX RI II

Přiložené soubory

2381699.pdf

Citovat

FRUHAUF, Sebastian; Dominic PUHRINGER; Michaela THAMHESL; Patricia FAJTL; Elisavet KUNZ-VEKIRU; Andreas HOBARTNER-GUSSL; Gerd SCHATZMAYR; Gerhard ADAM; Jiří DAMBORSKÝ; Kristina DJINOVIC-CARUGO; Zbyněk PROKOP a Wulf-Dieter MOLL. Bacterial Lactonases ZenA with Noncanonical Structural Features Hydrolyze the Mycotoxin Zearalenone. ACS Catalysis. WASHINGTON: AMER CHEMICAL SOC, 2024, roč. 14, č. 5, s. 3392-3410. ISSN 2155-5435. Dostupné z: https://doi.org/10.1021/acscatal.4c00271.

@article{2381699,
   author = {Fruhauf, Sebastian and Puhringer, Dominic and Thamhesl, Michaela and Fajtl, Patricia and KunzandVekiru, Elisavet and HobartnerandGussl, Andreas and Schatzmayr, Gerd and Adam, Gerhard and Damborský, Jiří and DjinovicandCarugo, Kristina and Prokop, Zbyněk and Moll, WulfandDieter},
   article_location = {WASHINGTON},
   article_number = {5},
   doi = {https://doi.org/10.1021/acscatal.4c00271},
   keywords = {zearalenone; mycotoxin; lactonase; carboxylesterase; hydrolase; kinetics; presteady-state; Rhodococcus erythropolis},
   language = {eng},
   issn = {2155-5435},
   journal = {ACS Catalysis},
   title = {Bacterial Lactonases ZenA with Noncanonical Structural Features Hydrolyze the Mycotoxin Zearalenone},
   url = {https://pubs.acs.org/doi/10.1021/acscatal.4c00271?ref=PDF},
   volume = {14},
   year = {2024}
}

TY  - JOUR
ID  - 2381699
AU  - Fruhauf, Sebastian - Puhringer, Dominic - Thamhesl, Michaela - Fajtl, Patricia - Kunz-Vekiru, Elisavet - Hobartner-Gussl, Andreas - Schatzmayr, Gerd - Adam, Gerhard - Damborský, Jiří - Djinovic-Carugo, Kristina - Prokop, Zbyněk - Moll, Wulf-Dieter
PY  - 2024
TI  - Bacterial Lactonases ZenA with Noncanonical Structural Features Hydrolyze the Mycotoxin Zearalenone
JF  - ACS Catalysis
VL  - 14
IS  - 5
SP  - 3392-3410
EP  - 3392-3410
PB  - AMER CHEMICAL SOC
SN  - 21555435
KW  - zearalenone
KW  - mycotoxin
KW  - lactonase
KW  - carboxylesterase
KW  - hydrolase
KW  - kinetics
KW  - presteady-state
KW  - Rhodococcus erythropolis
UR  - https://pubs.acs.org/doi/10.1021/acscatal.4c00271?ref=PDF
N2  - Zearalenone (ZEN) is a mycoestrogenic polyketide produced by Fusarium graminearum and other phytopathogenic members of the genus Fusarium. Contamination of cereals with ZEN is frequent, and hydrolytic detoxification with fungal lactonases has been explored. Here, we report the isolation of a bacterial strain, Rhodococcus erythropolis PFA D8-1, with ZEN hydrolyzing activity, cloning of the gene encoding alpha/beta hydrolase ZenA encoded on the linear megaplasmid pSFRL1, and biochemical characterization of nine homologues. Furthermore, we report site-directed mutagenesis as well as structural analysis of the dimeric ZenA(Re) of R. erythropolis and the more thermostable, tetrameric ZenA(Scfl) of Streptomyces coelicoflavus with and without bound ligands. The X-ray crystal structures not only revealed canonical features of alpha/beta hydrolases with a cap domain including a Ser-His-Asp catalytic triad but also unusual features including an uncommon oxyanion hole motif and a peripheral, short antiparallel beta-sheet involved in tetramer interactions. Presteady-state kinetic analyses for ZenA(Re) and ZenA(Scfl) identified balanced rate-limiting steps of the reaction cycle, which can change depending on temperature. Some new bacterial ZEN lactonases have lower K-M and higher k(cat) than the known fungal ZEN lactonases and may lend themselves to enzyme technology development for the degradation of ZEN in feed or food.
ER  -

FRUHAUF, Sebastian; Dominic PUHRINGER; Michaela THAMHESL; Patricia FAJTL; Elisavet KUNZ-VEKIRU; Andreas HOBARTNER-GUSSL; Gerd SCHATZMAYR; Gerhard ADAM; Jiří DAMBORSKÝ; Kristina DJINOVIC-CARUGO; Zbyněk PROKOP a Wulf-Dieter MOLL. Bacterial Lactonases ZenA with Noncanonical Structural Features Hydrolyze the Mycotoxin Zearalenone. \textit{ACS Catalysis}. WASHINGTON: AMER CHEMICAL SOC, 2024, roč.~14, č.~5, s.~3392-3410. ISSN~2155-5435. Dostupné z: https://doi.org/10.1021/acscatal.4c00271.

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