Biosynthesis of polyketide synthase extender units

YA Chan, AM Podevels, BM Kevany… - Natural product …, 2009 - pubs.rsc.org
Biosynthesis of polyketide synthase extender units - Natural Product Reports (RSC Publishing)
DOI:10.1039/B801658P Royal Society of Chemistry View PDF VersionPrevious ArticleNext …

Malonate metabolism: biochemistry, molecular biology, physiology, and industrial application

YS Kim - BMB Reports, 2002 - koreascience.kr
Malonate is a three-carbon dicarboxylic acid. It is well known as a competitive inhibitor of
succinate dehydrogenase. It occurs naturally in biological systems, such as legumes and …

The 1.75 Å crystal structure of acetyl-CoA synthetase bound to adenosine-5 '-propylphosphate and coenzyme A

AM Gulick, VJ Starai, AR Horswill, KM Homick… - Biochemistry, 2003 - ACS Publications
Acetyl-coenzyme A synthetase catalyzes the two-step synthesis of acetyl-CoA from acetate,
ATP, and CoA and belongs to a family of adenylate-forming enzymes that generate an acyl …

Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme A synthetases

JM Shockey, MS Fulda, J Browse - Plant physiology, 2003 - academic.oup.com
Acyl-activating enzymes are a diverse group of proteins that catalyze the activation of many
different carboxylic acids, primarily through the formation of a thioester bond. This group of …

Characterization of the Propionyl-CoA Synthetase (PrpE) Enzyme of Salmonella enterica:  Residue Lys592 Is Required for Propionyl-AMP Synthesis

AR Horswill, JC Escalante-Semerena - Biochemistry, 2002 - ACS Publications
The propionyl-CoA synthetase (PrpE) enzyme of Salmonella enterica catalyzes the first step
of propionate catabolism, ie, the activation of propionate to propionyl-CoA. The PrpE …

Validation of RetroPath, a computer‐aided design tool for metabolic pathway engineering

T Fehér, AG Planson, P Carbonell… - Biotechnology …, 2014 - Wiley Online Library
Metabolic engineering has succeeded in biosynthesis of numerous commodity or high value
compounds. However, the choice of pathways and enzymes used for production was many …

Transcriptomic Studies of the Effect of nod Gene-Inducing Molecules in Rhizobia: Different Weapons, One Purpose

I Jiménez-Guerrero, S Acosta-Jurado, P Del Cerro… - Genes, 2017 - mdpi.com
Simultaneous quantification of transcripts of the whole bacterial genome allows the analysis
of the global transcriptional response under changing conditions. RNA-seq and microarrays …

Identification of 4‐coumarate: coenzyme A ligase (4CL) substrate recognition domains

J Ehlting, JJK Shin, CJ Douglas - The Plant Journal, 2001 - Wiley Online Library
coumarate: CoA ligase (4CL), the last enzyme of the general phenylpropanoid pathway,
provides precursors for the biosynthesis of a large variety of plant natural products. 4 CL …

Mutagenesis evidence that the partial reactions of firefly bioluminescence are catalyzed by different conformations of the luciferase C-terminal domain

BR Branchini, TL Southworth, MH Murtiashaw… - Biochemistry, 2005 - ACS Publications
Firefly luciferase catalyzes two sequential partial reactions resulting in the emission of light.
The enzyme first catalyzes the adenylation of substrate luciferin with Mg-ATP followed by the …

Synthesis of adenylated molybdopterin: an essential step for molybdenum insertion

A Llamas, RR Mendel, G Schwarz - Journal of Biological Chemistry, 2004 - ASBMB
The molybdenum cofactor (Moco) is part of the active site of all molybdenum (Mo)-
dependent enzymes, except nitrogenase. Moco consists of molybdopterin (MPT), a …