Kinetic and structural studies of Trypanosoma and Leishmania phosphofructokinases show evolutionary divergence and identify AMP as a switch regulating glycolysis versus gluconeogenesis.
Adenosine Monophosphate
/ chemistry
Amino Acid Sequence
Animals
Biological Evolution
Catalytic Domain
Crystallography, X-Ray
Gluconeogenesis
Glycolysis
Guanosine Triphosphate
/ chemistry
Humans
Kinetics
Leishmania
/ enzymology
Models, Molecular
Phosphofructokinases
/ chemistry
Protein Conformation
Species Specificity
Substrate Specificity
Trypanosoma brucei brucei
/ enzymology
Leishmania
Trypanosoma
allostery
glycolysis
phosphofructokinase
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
07 2020
07 2020
Historique:
received:
16
09
2019
revised:
13
11
2019
accepted:
12
12
2019
pubmed:
16
12
2019
medline:
11
5
2021
entrez:
16
12
2019
Statut:
ppublish
Résumé
Trypanosomatids possess glycosome organelles that contain much of the glycolytic machinery, including phosphofructokinase (PFK). We present kinetic and structural data for PFK from three human pathogenic trypanosomatids, illustrating intriguing differences that may reflect evolutionary adaptations to differing ecological niches. The activity of Leishmania PFK - to a much larger extent than Trypanosoma PFK - is reliant on AMP for activity regulation, with 1 mm AMP increasing the L. infantum PFK (LiPFK) kcat/K
Identifiants
pubmed: 31838765
doi: 10.1111/febs.15177
pmc: PMC7383607
doi:
Substances chimiques
Adenosine Monophosphate
415SHH325A
Guanosine Triphosphate
86-01-1
Phosphofructokinases
EC 2.7.1 -
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2847-2861Subventions
Organisme : Medical Research Council
ID : MC_PC_16043
Pays : United Kingdom
Organisme : Wellcome
ID : 101784/Z/13/Z
Organisme : Wellcome Trust
ID : 106359
Pays : United Kingdom
Informations de copyright
© 2019 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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