Reaction mechanisms of thiamin diphosphate enzymes: defining states of ionization and tautomerization of the cofactor at individual steps

NS Nemeria, S Chakraborty, A Balakrishnan… - The FEBS …, 2009 - Wiley Online Library
We summarize the currently available information regarding the state of ionization and
tautomerization of the 4′‐aminopyrimidine ring of the thiamine diphosphate on enzymes …

Bacterial mandelic acid degradation pathway and its application in biotechnology

Q Wang, S Geng, L Wang, Z Wen… - Journal of Applied …, 2022 - academic.oup.com
Mandelic acid and its derivatives are an important class of chemical synthetic blocks, which
is widely used in drug synthesis and stereochemistry research. In nature, mandelic acid …

Catalysis in Enzymatic Decarboxylations: Comparison of Selected Cofactor-dependent and Cofactor-independent Examples.

F Jordan, H Patel - ACS catalysis, 2013 - ACS Publications
This review is focused on three types of enzymes decarboxylating very different
substrates:(1) thiamin diphosphate (ThDP)-dependent enzymes reacting with 2-oxo …

Substrate specificity in thiamin diphosphate-dependent decarboxylases

FH Andrews, MJ McLeish - Bioorganic chemistry, 2012 - Elsevier
Thiamin diphosphate (ThDP) is the biologically active form of vitamin B1, and ThDP-
dependent enzymes are found in all forms of life. The catalytic mechanism of this family …

Revealing donor substrate-dependent mechanistic control on DXPS, an enzyme in bacterial central metabolism

ML Johnston, CL Freel Meyers - Biochemistry, 2021 - ACS Publications
The thiamin diphosphate-dependent enzyme 1-deoxy-d-xylulose 5-phosphate synthase
(DXPS) catalyzes the formation of DXP from pyruvate (donor) and d-glyceraldehyde 3 …

The Catalytic Mechanism of Human Transketolase

M Prejanò, FE Medina, PA Fernandes… - …, 2019 - Wiley Online Library
We have computationally determined the catalytic mechanism of human transketolase (hTK)
using a cluster model approach and density functional theory calculations. We were able to …

Experimental observation of thiamin diphosphate-bound intermediates on enzymes and mechanistic information derived from these observations

F Jordan, NS Nemeria - Bioorganic Chemistry, 2005 - Elsevier
Thiamin diphosphate (ThDP), the vitamin B1 coenzyme, is an excellent representative of
coenzymes, which carry out electrophilic catalysis by forming a covalent complex with their …

Progress in the experimental observation of thiamin diphosphate-bound intermediates on enzymes and mechanistic information derived from these observations

F Jordan, NS Nemeria - Bioorganic chemistry, 2014 - Elsevier
Thiamin diphosphate (ThDP), the vitamin B1 coenzyme is an excellent representative of
coenzymes, which carry out electrophilic catalysis by forming a covalent complex with their …

QM/MM study of human transketolase: thiamine diphosphate activation mechanism and complete catalytic cycle

L Nauton, L Hecquet, V Théry - Journal of Chemical Information …, 2021 - ACS Publications
A computational model for human transketolase was proposed, showing that thiamine
diphosphate activation was based on His110 in place of His481 reported in yeast …

A dual conformation of the post-decarboxylation intermediate is associated with distinct enzyme states in mycobacterial KGD (α-ketoglutarate decarboxylase)

T Wagner, N Barilone, PM Alzari… - Biochemical …, 2014 - portlandpress.com
α-Ketoacid dehydrogenases are large multi-enzyme machineries that orchestrate the
oxidative decarboxylation of α-ketoacids with the concomitant production of acyl-CoA and …