BG Miller, R Wolfenden - Annual review of biochemistry, 2002 - annualreviews.org
▪ Abstract Enzymes are called upon to differ greatly in the difficulty of the tasks that they perform. The catalytic proficiency of an enzyme can be evaluated by comparing the second …
JA Gerlt, PC Babbitt - Genome biology, 2000 - Springer
The functional annotation of proteins identified in genome sequencing projects is based on similarities to homologs in the databases. As a result of the possible strategies for divergent …
T Li, L Huo, C Pulley, A Liu - Bioorganic Chemistry, 2012 - Elsevier
This review examines the mechanisms propelling cofactor-independent, organic cofactor- dependent and metal-dependent decarboxylase chemistry. Decarboxylation, the removal of …
TP Begley, C Kinsland, RA Mehl, A Osterman… - Vitamins & …, 2001 - Elsevier
The nicotinamide adenine dinucleotides (NAD, NADH, NADP, and NADPH) are essential cofactors in all living systems and function as hydride acceptors (NAD, NADP) and hydride …
S Rindfleisch, M Krull, J Uranga, T Schmidt… - Nature Catalysis, 2022 - nature.com
The origins of enzyme catalysis have been attributed to both transition-state stabilization as well as ground-state destabilization of the substrate. For the latter paradigm, the enzyme …
JA Gerlt, FM Raushel - Current opinion in chemical biology, 2003 - Elsevier
The (β/α) 8-barrel is the most common fold in structurally characterized enzymes. Whether the functionally diverse enzymes that share this fold are the products of either divergent or …
A Shurki, A Warshel - Advances in protein chemistry, 2003 - Elsevier
Publisher Summary This chapter focuses on the progress and the current state of structure/function correlations of biomolecules. One of the primary goals of modern …
TL Amyes, JP Richard - Biochemistry, 2013 - ACS Publications
Linus Pauling proposed that the large rate accelerations for enzymes are caused by the high specificity of the protein catalyst for binding the reaction transition state. The observation that …