Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
thioesterase family protein
This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily [1]. [1]. 15307895. The Hotdog fold: wrapping up a superfamily of thioesterases and. dehydratases.. Dillon SC, Bateman A;. BMC Bioinformatics 2004;5:109-109. (from Pfam)
hotdog domain-containing protein
This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyses the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyse the hydrolysis of other long chain fatty acyl-CoA thioesters. [1]. 9837940. The three-dimensional structure of 4-hydroxybenzoyl-CoA. thioesterase from Pseudomonas sp. Strain CBS-3.. Benning MM, Wesenberg G, Liu R, Taylor KL, Dunaway-Mariano D,. Holden HM;. J Biol Chem 1998;273:33572-33579.. [2]. 8805534. Structure of a dehydratase-isomerase from the bacterial pathway. for biosynthesis of unsaturated fatty acids: two catalytic. activities in one active site.. Leesong M, Henderson BS, Gillig JR, Schwab JM, Smith JL;. Structure 1996;4:253-264. (from Pfam)
acyl-ACP thioesterase domain-containing protein
This family consists of various acyl-acyl carrier protein (ACP) thioesterases (TE) these terminate fatty acyl group extension via hydrolysing an acyl group on a fatty acid [1]. These proteins are usually composed of a pair of tandem HotDog domains. This entry represents the N-terminal one of the pair. [1]. 7479856. Modification of the substrate specificity of an acyl-acyl. carrier protein thioesterase by protein engineering.. Yuan L, Voelker TA, Hawkins DJ;. Proc Natl Acad Sci U S A 1995;92:10639-10643.. [2]. 1621095. Fatty acid biosynthesis redirected to medium chains in. transgenic oilseed plants.. Voelker TA, Worrell AC, Anderson L, Bleibaum J, Fan C, Hawkins. DJ, Radke SE, Davies HM;. Science 1992;257:72-74.. [3]. 15531590. A structural model of the plant acyl-acyl carrier protein. thioesterase FatB comprised of two helix/4-stranded sheet. domains: The N-terminal domain containing residues that affect. specificity, the C-terminal domain containing catalytic. residues.. Mayer KM, Shanklin J;. J Biol Chem 2004; [Epub ahead of print] (from Pfam)
acyl-CoA thioesterase
acyl-CoA thioesterase catalyzes the hydrolysis of acyl-CoA esters to the free fatty acid and CoA; belongs to the Hotdog fold superfamily
YbgC/FadM family acyl-CoA thioesterase
This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon.
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on