Results 251 to 260 of about 89,834 (290)
ABSTRACT The role of the cell envelope‐associated Rv0132c/FGD2 from Mycobacterium tuberculosis has long been a subject of debate. Importantly, FGD2 is found only in pathogenic mycobacteria, making it a potential drug target. While some suggest it functions as a glucose‐6‐phosphate dehydrogenase, others propose it acts instead as an F420‐dependent ...
Adewale V. Aderemi +12 more
wiley +1 more source
ABSTRACT Proteins are built from modular domains that serve as fundamental units of structure and evolution. While individual domains have been extensively cataloged, their collective distribution across the lineages of life has remained poorly resolved.
Rui Guo +5 more
wiley +1 more source
The continuing significance of chiral agrochemicals
In the time frame 2018–2023, around 43% of the 35 chiral agrochemicals introduced to the market (herbicides, fungicides, insecticides, acaricides, and nematicides) contain one or more stereogenic centers in the molecule, and almost 69% of them have been marketed as racemic mixtures of enantiomers or stereoisomers.
Peter Jeschke
wiley +1 more source
ACYL CARRIER PROTEIN. 3. AN ENOYL HYDRASE SPECIFIC FOR ACYL CARRIER PROTEIN THIOESTERS.
P W, MAJERUS, A W, ALBERTS, P R, VAGELOS
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Archives of Biochemistry and Biophysics, 1984
The acyl-acyl carrier protein synthetase from Escherichia coli has been examined for its ability to specifically acylate acyl carrier protein (ACP) from higher plants in order to develop an assay for plant ACP, and to prepare labeled acyl-ACP of plant origin. It was found that the E.
T M, Kuo, J B, Ohlrogge
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The acyl-acyl carrier protein synthetase from Escherichia coli has been examined for its ability to specifically acylate acyl carrier protein (ACP) from higher plants in order to develop an assay for plant ACP, and to prepare labeled acyl-ACP of plant origin. It was found that the E.
T M, Kuo, J B, Ohlrogge
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Improved purification of acyl carrier protein
Analytical Biochemistry, 1980Abstract An improved method for the purification of acyl carrier protein from Escherichia coli is described. The method consists of four steps: a 2-propanol extraction, batch adsorption to DEAE-cellulose, ammonium sulfate fractionation, and acid precipitation.
C O, Rock, J E, Cronan
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Acyl carrier protein interacts with melittin
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1990Acyl carrier protein (ACP) from Escherichia coli has been shown to form complexes with melittin, a cationic peptide from bee venom. ACP is a small (Mr 8847), acidic, Ca2(+)-binding protein, which possesses some characteristics resembling those of regulatory Ca2(+)-binding proteins including interaction with melittin. Complexing between melittin and ACP
Ernst-Fonberg, Mary L. +2 more
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