Results 41 to 50 of about 89,501 (268)

Structure and substrate selectivity of the 750-kDa α6β6 holoenzyme of geranyl-CoA carboxylase. [PDF]

open access: yes, 2015
Geranyl-CoA carboxylase (GCC) is essential for the growth of Pseudomonas organisms with geranic acid as the sole carbon source. GCC has the same domain organization and shares strong sequence conservation with the related biotin-dependent carboxylases 3 ...
Huang, Christine S   +4 more
core   +2 more sources

Machine Learning Accelerates Crystallization for Structure Determination

open access: yesAngewandte Chemie, EarlyView.
Single‐crystal x‐ray diffraction (SCXRD) is often constrained by the difficulty of obtaining suitable crystals. Here, a machine learning‐accelerated co‐crystal discovery workflow is established for a crystalline mate strategy that achieves over 95% prediction accuracy and experimentally delivers 114 co‐crystals from 120 candidates.
Cui‐Zhou Luan   +10 more
wiley   +2 more sources

In silico identification of potential inhibitors of acyl carrier protein reductase and acetyl CoA carboxylase of Plasmodium falciparum in antimalarial therapy

open access: yesFrontiers in Drug Discovery, 2023
Malaria caused by Plasmodium falciparum, remains one of the most fatal parasitic diseases that has affected nearly a third of the world’s population. The major impediment to the treatment of malaria is the emergence of resistance of the P.
Elliasu Y. Salifu   +5 more
doaj   +1 more source

Activation of immobilized acetyl-Coenzyme A carboxylase [PDF]

open access: yesBiochemical Journal, 1978
Partially purified acetyl-CoA carboxylase was covalently bound to a Sepharose 4B matrix. Although aggregation was thus prevented, the enzymic activity was stimulated by citrate and isocitrate.
A D, Landman, J, Lampert
openaire   +2 more sources

Insights into the Ecological Roles and Evolution of Methyl-Coenzyme M Reductase-Containing Hot Spring Archaea [PDF]

open access: yes, 2019
Several recent studies have shown the presence of genes for the key enzyme associated with archaeal methane/alkane metabolism, methyl-coenzyme M reductase (Mcr), in metagenome-assembled genomes (MAGs) divergent to existing archaeal lineages.
Chen, Ya-Ting   +17 more
core   +3 more sources

Determination of acetyl coenzyme A. Interference by a contaminant in malate dehydrogenase

open access: yesJournal of Lipid Research, 1972
Spectrophotometric determinations of acetyl CoA with malate dehydrogenase and citrate synthase are likely to overestimate the amount of acetyl CoA in solutions containing acetoacetyl CoA, since commercial preparations of malate dehydrogenase may contain ...
I. Mulder
doaj   +1 more source

Novel Cryptosporidium genotype in wild Australian mice (Mus domesticus) [PDF]

open access: yes, 2007
A total of 250 mouse fecal specimens collected from crop farms in Queensland, Australia, were screened for the presence of Cryptosporidium spp. using PCR.
Boxell, A.   +4 more
core   +3 more sources

Stereoselective Biotransformation: Transfer of Learning to Advance Drug Metabolism and Biocatalysis

open access: yesAngewandte Chemie, EarlyView.
Understanding stereoselective biotransformations has implications for predicting drug disposition and response and may also inspire novel biocatalytic and biomimetic strategies to address challenges in metabolite and API synthesis. ABSTRACT Chirality is an important determinant of drug action, as enantiomers can exhibit markedly different ...
Grace A. Okunlola, Godwin A. Aleku
wiley   +2 more sources

AASLD practice guidance on drug, herbal, and dietary supplement–induced liver injury

open access: yes, 2022
Hepatology, EarlyView.
Robert J. Fontana   +6 more
wiley   +1 more source

Regulation of AMP-activated protein kinase and acetyl-CoA carboxylase phosphorylation by palmitate in skeletal muscle cells

open access: yesJournal of Lipid Research, 2006
The purpose of this study was to investigate the effects of long-chain fatty acids (LCFAs) on AMP-activated protein kinase (AMPK) and acetyl-coenzyme A carboxylase (ACC) phosphorylation and β-oxidation in skeletal muscle.
S. Fediuc, M.P. Gaidhu, R.B. Ceddia
doaj   +1 more source

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