Expression of a heptelidic acid-insensitive recombinant GAPDH from Trichoderma virens, and its biochemical and biophysical characterization.
GAPDH
Koningic acid
Protein purification
Secondary metabolism
Trichoderma virens
Journal
Protein expression and purification
ISSN: 1096-0279
Titre abrégé: Protein Expr Purif
Pays: United States
ID NLM: 9101496
Informations de publication
Date de publication:
11 2020
11 2020
Historique:
received:
07
04
2020
revised:
08
06
2020
accepted:
26
06
2020
pubmed:
19
7
2020
medline:
29
1
2021
entrez:
19
7
2020
Statut:
ppublish
Résumé
Trichoderma virens genome harbors two isoforms of GAPDH, one (gGPD) involved in glycolysis and the other one (vGPD) in secondary metabolism. vGPD is expressed as part of the "vir" cluster responsible for the biosynthesis of volatile sesquiterpenes. The secondary metabolism-associated GAPDH is tolerant to the anti-cancer metabolite heptelidic acid (HA), produced by T. virens. Characterizing the HA-tolerant form of GAPDH, thus has implications in cancer therapy. In order to get insight into the mechanism of HA-tolerance of vGPD, we have purified recombinant form of this protein. The protein displays biochemical and biophysical characteristics analogous to the gGPD isoform. It exists as a tetramer with Tm of about 56.5 °C, and displays phosphorylation enzyme activity with Km and Kcat of 0.38 mM and 2.55 sec
Identifiants
pubmed: 32681951
pii: S1046-5928(20)30288-6
doi: 10.1016/j.pep.2020.105697
pii:
doi:
Substances chimiques
Fungal Proteins
0
Recombinant Proteins
0
Sesquiterpenes
0
heptelidic acid
57710-57-3
Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)
EC 1.2.1.12
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
105697Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.