Enzymes
UniProtKB help_outline | 4 proteins |
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- Name help_outline 1-hexadecanoylglycerone 3-phosphate Identifier CHEBI:58303 Charge -2 Formula C19H35O7P InChIKeyhelp_outline MLWXSIMRTQAWHY-UHFFFAOYSA-L SMILEShelp_outline CCCCCCCCCCCCCCCC(=O)OCC(=O)COP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 15 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline hexadecan-1-ol Identifier CHEBI:16125 (CAS: 36653-82-4) help_outline Charge 0 Formula C16H34O InChIKeyhelp_outline BXWNKGSJHAJOGX-UHFFFAOYSA-N SMILEShelp_outline C(CCCCCCCCCCCCCCC)O 2D coordinates Mol file for the small molecule Search links Involved in 14 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 1-O-hexadecylglycerone 3-phosphate Identifier CHEBI:77429 Charge -2 Formula C19H37O6P InChIKeyhelp_outline KFZPNXQHABIFMZ-UHFFFAOYSA-L SMILEShelp_outline CCCCCCCCCCCCCCCCOCC(=O)COP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline hexadecanoate Identifier CHEBI:7896 (Beilstein: 3589907; CAS: 143-20-4) help_outline Charge -1 Formula C16H31O2 InChIKeyhelp_outline IPCSVZSSVZVIGE-UHFFFAOYSA-M SMILEShelp_outline CCCCCCCCCCCCCCCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 92 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:40659 | RHEA:40660 | RHEA:40661 | RHEA:40662 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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The mechanism of alkyldihydroxyacetone-P synthase. Formation of [3H]H2O from acyl[1-R-3H]dihydroxyacetone-P by purified alkyldihydroxyacetone-P synthase in the absence of acylhydrolase activity.
Brown A.J., Snyder F.
Alkyldihydroxyacetone-P (alkyl-DHAP) synthase catalyzes the exchange of the fatty acid esterified to C-1 of the DHAP portion of acyl-DHAP for a fatty alcohol to form 1-O-alkyl-DHAP, the first ether-linked intermediate in ether lipid biosynthesis. Another characteristic of the reaction is the excha ... >> More
Alkyldihydroxyacetone-P (alkyl-DHAP) synthase catalyzes the exchange of the fatty acid esterified to C-1 of the DHAP portion of acyl-DHAP for a fatty alcohol to form 1-O-alkyl-DHAP, the first ether-linked intermediate in ether lipid biosynthesis. Another characteristic of the reaction is the exchange of the pro-R hydrogen at C-1. We have investigated this hydrogen exchange using palmitoyl-[1-R-3H]DHAP and a 1000-fold purified preparation of alkyl-DHAP synthase. We found a small but significant pro-R hydrogen exchange in the absence of the co-substrate, fatty alcohol. When [14C]hexadecanol was added, the increase in pro-R 3H exchange was equal to the [14C]hexadecyl-DHAP formed. Addition of [14C]palmitic acid resulted in an increase in pro-R 3H exchange that matched the formation of [14C]palmitoyl-DHAP by the acyl exchange activity of alkyl-DHAP synthase. Furthermore, although whole microsomes contain at least two acyl hydrolases for acyl-DHAP, purified preparations of alkyl-DHAP synthase do not form DHAP from acyl-DHAP. These results are discussed with respect to data obtained from other laboratories using whole microsomes and in support of our proposed ping-pong mechanism for alkyl-DHAP synthase. << Less
J. Biol. Chem. 258:4184-4189(1983) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Assay and properties of the enzyme catalyzing the biosynthesis of 1-O-alkyl dihydroxyacetone 3-phosphate.
Davis P.A., Hajra A.K.
Arch Biochem Biophys 211:20-29(1981) [PubMed] [EuropePMC]
This publication is cited by 9 other entries.
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Ether lipid synthesis: purification and identification of alkyl dihydroxyacetone phosphate synthase from guinea-pig liver.
Zomer A.W., de Weerd W.F., Langeveld J., van den Bosch H.
Alkyl-dihydroxyacetone phosphate synthase, the second enzyme involved in ether phospholipid biosynthesis from dihydroxyacetone phosphate and responsible for glycero-ether bond formation, has been purified from guinea-pig liver. Alkyl-dihydroxyacetone phosphate synthase was solubilized from a membr ... >> More
Alkyl-dihydroxyacetone phosphate synthase, the second enzyme involved in ether phospholipid biosynthesis from dihydroxyacetone phosphate and responsible for glycero-ether bond formation, has been purified from guinea-pig liver. Alkyl-dihydroxyacetone phosphate synthase was solubilized from a membrane fraction prepared from an enriched peroxisome fraction with Triton X-100 and potassium chloride. The solubilized enzyme was further purified by chromatography on QAE-Sephadex, Matrex Red, Phosphocellulose and Concanavalin A. Upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis alkyl-dihydroxyacetone phosphate synthase appears as a 65 kDa band. Chromatofocusing revealed an isoelectric point of pH 5.9 for the enzyme. The pH optimum of alkyl-dihydroxyacetone phosphate synthase was found to be between pH 7 and 8 in a 50 mM potassium phosphate buffer. The specific activity of the enzyme was estimated to be at least 350 nmol.min-1.mg-1, corresponding to a purification of at least 13,000-fold. << Less
Biochim. Biophys. Acta 1170:189-196(1993) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Characterization of recombinant guinea pig alkyl-dihydroxyacetonephosphate synthase expressed in Escherichia coli. Kinetics, chemical modification and mutagenesis.
de Vet E.C., van den Bosch H.
A recombinant form of guinea pig alkyl-dihydroxyacetonephosphate synthase, a key enzyme in the biosynthesis of ether phospholipids, was characterized. Kinetic analysis yielded evidence that the enzyme operates by a ping-pong rather than a sequential mechanism. Enzyme activity was irreversibly inhi ... >> More
A recombinant form of guinea pig alkyl-dihydroxyacetonephosphate synthase, a key enzyme in the biosynthesis of ether phospholipids, was characterized. Kinetic analysis yielded evidence that the enzyme operates by a ping-pong rather than a sequential mechanism. Enzyme activity was irreversibly inhibited by N-ethylmaleimide, p-bromophenacylbromide and 2,4-dinitrofluorobenzene. The enzyme could be protected against the inactivation by either of these three compounds by the presence of saturating amounts of the substrate palmitoyl-dihydroxyacetonephosphate. The rate of inactivation of the enzyme by p-bromophenacylbromide was strongly pH dependent and the highest at alkaline conditions. Collectively, these results are indicative of cysteine, histidine and lysine residues, respectively, at or close to the active site. The divalent cations Mg2+, Zn2+ and Mn2+ were found to be inhibitors of enzymatic activity, whereas Ca2+ had no effect. Mutational analysis showed that histidine 617 is an essential amino acid for enzymatic activity: replacement of this residue by alanine resulted in complete loss of enzymatic activity. A recombinant enzyme with the C-terminal five amino acids deleted was shown to be inactive, indicating an important role of the C-terminus for catalytic activity. << Less
Biochim. Biophys. Acta 1436:299-306(1999) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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The native molecular size of alkyl-dihydroxyacetonephosphate synthase and dihydroxyacetonephosphate acyltransferase.
Biermann J., Schoonderwoerd K., Hom M.L., Luthjens L.H., Van den Bosch H.
Dihydroxyacetonephosphate acyltransferase (DHAP-acyltransferase) and alkyl-dihydroxyacetonephosphate synthase (alkyl-DHAP synthase) are the first two enzymes involved in the biosynthesis of ether phospholipids. Both peroxisomal enzymes have recently been purified to homogeneity and their molecular ... >> More
Dihydroxyacetonephosphate acyltransferase (DHAP-acyltransferase) and alkyl-dihydroxyacetonephosphate synthase (alkyl-DHAP synthase) are the first two enzymes involved in the biosynthesis of ether phospholipids. Both peroxisomal enzymes have recently been purified to homogeneity and their molecular weights under denaturing conditions were reported. To determine the in situ functional size of both enzymes, radiation inactivation experiments were performed. Alkyl-DHAP synthase showed single exponential decays, both when enzymatic activity and when immunoreactive protein levels were measured, from which target sizes of 79+/-2 kDa and 78+/-4 kDa, respectively, were calculated. DHAP-acyltransferase activity increased at lower doses and decayed upon further irradiation with an apparent target size of 62+/-7 kDa. We conclude from these data that the functional unit sizes for both enzymes in situ are represented by their single polypeptide chains. << Less
Biochim Biophys Acta 1393:137-142(1998) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.