Reaction participants Show >> << Hide
-
Namehelp_outline
a (3R)-hydroxyacyl-[ACP]
Identifier
RHEA-COMP:9945
Reactive part
help_outline
- Name help_outline (3R)-hydroxyacyl-pantetheine-4-phosphorylserine residue Identifier CHEBI:78827 Charge -1 Formula C17H28N3O10PSR SMILEShelp_outline CC(C)(COP([O-])(=O)OC[C@H](N-*)C(-*)=O)[C@@H](O)C(=O)NCCC(=O)NCCSC(=O)C[C@H](O)[*] 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
-
Namehelp_outline
a (2E)-enoyl-[ACP]
Identifier
RHEA-COMP:9925
Reactive part
help_outline
- Name help_outline O-(S-(2E)-enoylpantetheine-4ʼ-phosphoryl)-L-serine residue Identifier CHEBI:78784 Charge -1 Formula C17H26N3O9PSR SMILEShelp_outline CC(C)(COP([O-])(=O)OC[C@H](N-*)C(-*)=O)[C@@H](O)C(=O)NCCC(=O)NCCSC(=O)\C=C\[*] 2D coordinates Mol file for the small molecule Search links Involved in 36 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,148 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:13097 | RHEA:13098 | RHEA:13099 | RHEA:13100 | |
---|---|---|---|---|
Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
|
|||
EC numbers help_outline | ||||
Gene Ontology help_outline | ||||
KEGG help_outline | ||||
MetaCyc help_outline | ||||
EcoCyc help_outline |
Related reactions help_outline
Specific form(s) of this reaction
Publications
-
An ancient genetic link between vertebrate mitochondrial fatty acid synthesis and RNA processing.
Autio K.J., Kastaniotis A.J., Pospiech H., Miinalainen I.J., Schonauer M.S., Dieckmann C.L., Hiltunen J.K.
In bacteria, functionally related gene products are often encoded by a common transcript. Such polycistronic transcripts are rare in eukaryotes. Here we isolated several clones from human cDNA libraries, which rescued the respiratory-deficient phenotype of a yeast mitochondrial 3-hydroxyacyl thioe ... >> More
In bacteria, functionally related gene products are often encoded by a common transcript. Such polycistronic transcripts are rare in eukaryotes. Here we isolated several clones from human cDNA libraries, which rescued the respiratory-deficient phenotype of a yeast mitochondrial 3-hydroxyacyl thioester dehydratase 2 (htd2) mutant strain. All complementing cDNAs were derived from the RPP14 transcript previously described to encode the RPP14 subunit of the human ribonuclease P (RNase P) complex. We identified a second, 3' open reading frame (ORF) on the RPP14 transcript encoding a protein showing similarity to known dehydratases and hydratase 2 enzymes. The protein was localized in mitochondria, and the recombinant enzyme exhibited (3R)-specific hydratase 2 activity. Based on our results, we named the protein human 3-hydroxyacyl-thioester dehydratase 2 (HsHTD2), which is involved in mitochondrial fatty acid synthesis. The bicistronic arrangement of RPP14 and HsHTD2, as well as the general exon structure of the gene, is conserved in vertebrates from fish to humans, indicating a genetic link conserved for 400 million years between RNA processing and mitochondrial fatty acid synthesis. << Less
-
Crystallization and preliminary X-ray analysis of beta-hydroxydecanoyl thiol ester dehydrase from Escherichia coli.
Sharma A., Henderson B.S., Schwab J.M., Smith J.L.
Escherichia coli beta-hydroxydecanoyl thiol ester dehydrase, a key enzyme for the biosynthesis of unsaturated fatty acids in E. coli, has been crystallized by the vapor diffusion method at pH 5.0-5.5 using 20% (w/v) polyethylene glycol (molecular weight 8000) as a precipitant. Two crystal forms ha ... >> More
Escherichia coli beta-hydroxydecanoyl thiol ester dehydrase, a key enzyme for the biosynthesis of unsaturated fatty acids in E. coli, has been crystallized by the vapor diffusion method at pH 5.0-5.5 using 20% (w/v) polyethylene glycol (molecular weight 8000) as a precipitant. Two crystal forms have been characterized, and both diffract to at least 1.6 A. The orthorhombic crystals belong to space group P2(1)2(1)2(1), with cell constants of a = 68.4 A, b = 87.3 A, and c = 60.3 A. Monoclinic crystals are of space group C2, with a = 131.9 A, b = 71.5 A, c = 92.5 A, and beta = 103.5 degrees. << Less
-
Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis.
Heath R.J., Rock C.O.
There are two genes, fabA and fabZ, encoding beta-hydroxyacyl-acyl carrier protein (ACP) dehydratases that function in the dissociated, type II fatty acid synthase system of Escherichia coli. We have investigated their roles in fatty acid synthesis by purifying the two proteins and reconstituting ... >> More
There are two genes, fabA and fabZ, encoding beta-hydroxyacyl-acyl carrier protein (ACP) dehydratases that function in the dissociated, type II fatty acid synthase system of Escherichia coli. We have investigated their roles in fatty acid synthesis by purifying the two proteins and reconstituting cycles of fatty acid synthesis in vitro using five other purified proteins. FabA and FabZ exhibited broad, overlapping chain length specificities. The FabZ dehydratase efficiently catalyzed the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. FabA was most active on intermediate chain length beta-hydroxyacyl-ACPs and also possessed significant activity toward both short and long chain saturated beta-hydroxyacyl-ACPs. Significantly, FabA was virtually inactive in the dehydration of long chain unsaturated beta-hydroxyacyl-ACP. The introduction of the double bond at the 10-carbon stage of fatty acid synthesis by FabA was only detected in the presence of beta-ketoacyl-ACP synthase I (FabB). A yeast two-hybrid analysis failed to detect an interaction between FabA and FabB, therefore the channeling of intermediates toward unsaturated fatty acid synthesis by FabB was attributed to the affinity of the condensing enzyme for cis-decenoyl-ACP. The broad substrate specificity of FabZ coupled with the inactivity of FabA toward a long chain unsaturated beta-hydroxyacyl-ACP provides a biochemical explanation for the phenotypes of cells with genetically altered levels of the two dehydratases. << Less
J. Biol. Chem. 271:27795-27801(1996) [PubMed] [EuropePMC]
This publication is cited by 23 other entries.
-
Fatty acid synthesis and elongation in yeast.
Tehlivets O., Scheuringer K., Kohlwein S.D.
Fatty acids are essential compounds in the cell. Since the yeast Saccharomyces cerevisiae does not feed typically on fatty acids, cellular function and growth relies on endogenous synthesis. Since all cellular organelles are involved in-- or dependent on--fatty acid synthesis, multiple levels of c ... >> More
Fatty acids are essential compounds in the cell. Since the yeast Saccharomyces cerevisiae does not feed typically on fatty acids, cellular function and growth relies on endogenous synthesis. Since all cellular organelles are involved in-- or dependent on--fatty acid synthesis, multiple levels of control may exist to ensure proper fatty acid composition and homeostasis. In this review, we summarize what is currently known about enzymes involved in cellular fatty acid synthesis and elongation, and discuss potential links between fatty acid metabolism, physiology and cellular regulation. << Less
Biochim Biophys Acta 1771:255-270(2007) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.