Plant Nitrilase Homologues in Fungi: Phylogenetic and Functional Analysis with Focus on Nitrilases in Trametes versicolor and Agaricus bisporus

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F20%3A00532967" target="_blank" >RIV/61388971:_____/20:00532967 - isvavai.cz</a>

Alternative codes found

RIV/68407700:21460/20:00348820

Result on the web

<a href="https://www.mdpi.com/1420-3049/25/17/3861" target="_blank" >https://www.mdpi.com/1420-3049/25/17/3861</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/molecules25173861" target="_blank" >10.3390/molecules25173861</a>

Result language

angličtina

Original language name

Plant Nitrilase Homologues in Fungi: Phylogenetic and Functional Analysis with Focus on Nitrilases in Trametes versicolor and Agaricus bisporus

Original language description

Fungi contain many plant-nitrilase (NLase) homologues according to database searches. In this study, enzymes NitTv1 fromTrametes versicolorand NitAb fromAgaricus bisporuswere purified and characterized as the representatives of this type of fungal NLase. Both enzymes were slightly more similar to NIT4 type than to NIT1/NIT2/NIT3 type of plant NLases in terms of their amino acid sequences. Expression of the synthetic genes inEscherichia coliOrigami B (DE3) was induced with 0.02 mM isopropyl beta-D-1-thiogalactopyranoside at 20 degrees C. Purification of NitTv1 and NitAb by cobalt affinity chromatography gave ca. 6.6 mg and 9.6 mg of protein per 100 mL of culture medium, respectively. Their activities were determined with 25 mM of nitriles in 50 mM Tris/HCl buffer, pH 8.0, at 30 degrees C. NitTv1 and NitAb transformed beta-cyano-L-alanine (beta-CA) with the highest specific activities (ca. 132 and 40 U mg(-1), respectively) similar to plant NLase NIT4. beta-CA was transformed into Asn and Asp as in NIT4 but at lower Asn:Asp ratios. The fungal NLases also exhibited significant activities for (aryl)aliphatic nitriles such as 3-phenylpropionitrile, cinnamonitrile and fumaronitrile (substrates of NLase NIT1). NitTv1 was more stable than NitAb (at pH 5-9 vs. pH 5-7). These NLases may participate in plant-fungus interactions by detoxifying plant nitriles and/or producing plant hormones. Their homology models elucidated the molecular interactions with various nitriles in their active sites.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2020

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Molecules

ISSN

1420-3049

e-ISSN

—

Volume of the periodical

25

Issue of the periodical within the volume

17

Country of publishing house

CH - SWITZERLAND

Number of pages

20

Pages from-to

3861

UT code for WoS article

000570398700001

EID of the result in the Scopus database

2-s2.0-85090004951