|
|
Displaying entries 51-57 of 57.
<< Previous | Next >> 
Printable version
| EC | 3.1.2.22 | ||||||||
| Accepted name: | palmitoyl[protein] hydrolase | ||||||||
| Reaction: | palmitoyl[protein] + H2O = palmitate + protein | ||||||||
| Other name(s): | palmitoyl-protein thioesterase; palmitoyl-(protein) hydrolase | ||||||||
| Systematic name: | palmitoyl[protein] hydrolase | ||||||||
| Comments: | Specific for long-chain thioesters of fatty acids. Hydrolyses fatty acids from S-acylated cysteine residues in proteins, palmitoyl cysteine and palmitoyl-CoA. | ||||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 150605-49-5 | ||||||||
| References: |
| ||||||||
| EC | 3.1.2.26 | ||||||||
| Transferred entry: | bile-acid-CoA hydrolase. Now EC 2.8.3.25, bile acid CoA transferase | ||||||||
| EC | 3.5.1.60 | ||||||||
| Accepted name: | N-(long-chain-acyl)ethanolamine deacylase | ||||||||
| Reaction: | N-(long-chain-acyl)ethanolamine + H2O = a long-chain carboxylate + ethanolamine | ||||||||
| Other name(s): | NAAA (gene name); N-acylethanolamine amidohydrolase; acylethanolamine amidase | ||||||||
| Systematic name: | N-(long-chain-acyl)ethanolamine amidohydrolase | ||||||||
| Comments: | This lysosomal enzyme acts best on palmitoyl ethanolamide, with lower activity on other N-(long-chain-acyl)ethanolamines. It is only active at acidic pH. Unlike EC 3.5.1.99, fatty acid amide hydrolase, it does not act on primary amides such as oleamide, and has only a marginal activity with anandamide. The enzyme is translated as an inactive proenzyme, followed by autocatalytic cleavage into two subunits that reassociate to form an active heterodimeric complex. | ||||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 99283-61-1 | ||||||||
| References: |
| ||||||||
| EC | 4.2.1.61 | ||||||||
| Deleted entry: | 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase. The reaction described is covered by EC 4.2.1.59. | ||||||||
| EC | 4.2.1.134 | ||||||||
| Accepted name: | very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase | ||||||||
| Reaction: | a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain trans-2,3-dehydroacyl-CoA + H2O | ||||||||
| Glossary: | a very-long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 23 or more carbon atoms. | ||||||||
| Other name(s): | PHS1 (gene name); PAS2 (gene name) | ||||||||
| Systematic name: | very-long-chain (3R)-3-hydroxyacyl-CoA hydro-lyase | ||||||||
| Comments: | This is the third component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long chain acyl CoAs. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase. | ||||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||
| References: |
| ||||||||
| EC | 6.2.1.3 | ||||||||
| Accepted name: | long-chain-fatty-acid—CoA ligase | ||||||||
| Reaction: | ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA | ||||||||
| Glossary: | a long-chain-fatty acid = a fatty acid with an aliphatic chain of 13-22 carbons. | ||||||||
| Other name(s): | acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetase; acyl coenzyme A synthetase; acyl-CoA ligase; palmitoyl coenzyme A synthetase; thiokinase; palmitoyl-CoA ligase; acyl-coenzyme A ligase; fatty acid CoA ligase; long-chain fatty acyl coenzyme A synthetase; oleoyl-CoA synthetase; stearoyl-CoA synthetase; long chain fatty acyl-CoA synthetase; long-chain acyl CoA synthetase; fatty acid elongase; LCFA synthetase; pristanoyl-CoA synthetase; ACS3; long-chain acyl-CoA synthetase I; long-chain acyl-CoA synthetase II; fatty acyl-coenzyme A synthetase; long-chain acyl-coenzyme A synthetase; FAA1 | ||||||||
| Systematic name: | long-chain fatty acid:CoA ligase (AMP-forming) | ||||||||
| Comments: | Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. The liver enzyme acts on acids from C6 to C20; that from brain shows high activity up to C24. | ||||||||
| Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-18-7 | ||||||||
| References: |
| ||||||||
| EC | 6.2.1.57 | ||||||||
| Accepted name: | long-chain fatty acid adenylase/transferase FadD23 | ||||||||
| Reaction: | (1) ATP + stearate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + diphosphate + a stearoyl-[(hydroxy)phthioceranic acid synthase] (overall reaction) (1a) ATP + stearate = diphosphate + (stearoyl)adenylate (1b) (stearoyl)adenylate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + a stearoyl-[(hydroxy)phthioceranic acid synthase] (2) ATP + palmitate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + diphosphate + a palmitoyl-[(hydroxy)phthioceranic acid synthase] (overall reaction) (2a) ATP + palmitate = diphosphate + (palmitoyl)adenylate (2b) (palmitoyl)adenylate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + a palmitoyl-[(hydroxy)phthioceranic acid synthase] |
||||||||
| Other name(s): | fadD23 (gene name); long-chain fatty acid adenylyltransferase FadD23 | ||||||||
| Systematic name: | palmitate:holo-[(hydroxy)phthioceranic acid synthase] ligase | ||||||||
| Comments: | This mycobacterial enzyme activates palmitate and stearate by adenylation, followed by their loading onto the polyketide synthase EC 2.3.1.287, phthioceranic/hydroxyphthioceranic acid synthase. | ||||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||
| References: |
| ||||||||