node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Acnat1 | Acnat2 | ENSMUSP00000092702 | ENSMUSP00000080256 | Acyl-coenzyme A amino acid N-acyltransferase 1; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine. | Acyl-coenzyme A amino acid N-acyltransferase 2; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine (By similarity). | 0.907 |
Acnat1 | Acot8 | ENSMUSP00000092702 | ENSMUSP00000099383 | Acyl-coenzyme A amino acid N-acyltransferase 1; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine. | Acyl-coenzyme A thioesterase 8; Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Acyl-coenzyme A thioesterase 8/ACOT8 display no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs. Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains. Moreover, it catalyz [...] | 0.924 |
Acnat1 | Baat | ENSMUSP00000092702 | ENSMUSP00000041983 | Acyl-coenzyme A amino acid N-acyltransferase 1; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine. | Bile acid-CoA:amino acid N-acyltransferase; Catalyzes the amidation of bile acids (BAs) with the amino acid taurine. Selective for taurine conjugation of cholyl CoA and only taurine-conjugated BAs are found in bile. Amidation of BAs in the liver with taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism (By similarity). This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates l [...] | 0.908 |
Acnat1 | Csad | ENSMUSP00000092702 | ENSMUSP00000023805 | Acyl-coenzyme A amino acid N-acyltransferase 1; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine. | Cysteine sulfinic acid decarboxylase; Catalyzes the decarboxylation of L-aspartate, 3-sulfino-L- alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine and taurine, respectively. The preferred substrate is 3- sulfino-L-alanine. Does not exhibit any decarboxylation activity toward glutamate. | 0.932 |
Acnat1 | Gad1 | ENSMUSP00000092702 | ENSMUSP00000092539 | Acyl-coenzyme A amino acid N-acyltransferase 1; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine. | Glutamate decarboxylase 1; Catalyzes the production of GABA; Belongs to the group II decarboxylase family. | 0.902 |
Acnat1 | Gad2 | ENSMUSP00000092702 | ENSMUSP00000028123 | Acyl-coenzyme A amino acid N-acyltransferase 1; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine. | Glutamate decarboxylase 2; Catalyzes the production of GABA. | 0.902 |
Acnat1 | Ggt1 | ENSMUSP00000092702 | ENSMUSP00000006508 | Acyl-coenzyme A amino acid N-acyltransferase 1; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine. | Glutathione hydrolase 1 heavy chain; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione [...] | 0.900 |
Acnat1 | Ggt6 | ENSMUSP00000092702 | ENSMUSP00000075773 | Acyl-coenzyme A amino acid N-acyltransferase 1; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine. | Glutathione hydrolase 6 heavy chain; Cleaves glutathione conjugates; Belongs to the gamma-glutamyltransferase family. | 0.900 |
Acnat1 | Scp2 | ENSMUSP00000092702 | ENSMUSP00000030340 | Acyl-coenzyme A amino acid N-acyltransferase 1; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine. | Non-specific lipid-transfer protein; Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis. | 0.936 |
Acnat1 | Slc27a5 | ENSMUSP00000092702 | ENSMUSP00000032539 | Acyl-coenzyme A amino acid N-acyltransferase 1; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine. | Bile acyl-CoA synthetase; Acyl-CoA synthetase that catalyzes the activation of bile acids via formation of bile acid CoA thioesters which is necessary for their subsequent conjugation with glycine or taurine. Catalyzes the activation of the primary bile acid, cholic acid. Both primary bile acid (chenodeoxycholic acid) and secondary bile acids (deoxycholic acid and lithocholic acid) are the principal substrates (By similarity). Also exhibits acyl CoA synthetase activity that activates very long-chain fatty acids (VLCFAs) by catalyzing the formation of fatty acyl-CoA (By similarity). In [...] | 0.962 |
Acnat2 | Acnat1 | ENSMUSP00000080256 | ENSMUSP00000092702 | Acyl-coenzyme A amino acid N-acyltransferase 2; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine (By similarity). | Acyl-coenzyme A amino acid N-acyltransferase 1; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine. | 0.907 |
Acnat2 | Acot8 | ENSMUSP00000080256 | ENSMUSP00000099383 | Acyl-coenzyme A amino acid N-acyltransferase 2; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine (By similarity). | Acyl-coenzyme A thioesterase 8; Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Acyl-coenzyme A thioesterase 8/ACOT8 display no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs. Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains. Moreover, it catalyz [...] | 0.922 |
Acnat2 | Baat | ENSMUSP00000080256 | ENSMUSP00000041983 | Acyl-coenzyme A amino acid N-acyltransferase 2; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine (By similarity). | Bile acid-CoA:amino acid N-acyltransferase; Catalyzes the amidation of bile acids (BAs) with the amino acid taurine. Selective for taurine conjugation of cholyl CoA and only taurine-conjugated BAs are found in bile. Amidation of BAs in the liver with taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism (By similarity). This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates l [...] | 0.928 |
Acnat2 | Csad | ENSMUSP00000080256 | ENSMUSP00000023805 | Acyl-coenzyme A amino acid N-acyltransferase 2; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine (By similarity). | Cysteine sulfinic acid decarboxylase; Catalyzes the decarboxylation of L-aspartate, 3-sulfino-L- alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine and taurine, respectively. The preferred substrate is 3- sulfino-L-alanine. Does not exhibit any decarboxylation activity toward glutamate. | 0.929 |
Acnat2 | Gad1 | ENSMUSP00000080256 | ENSMUSP00000092539 | Acyl-coenzyme A amino acid N-acyltransferase 2; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine (By similarity). | Glutamate decarboxylase 1; Catalyzes the production of GABA; Belongs to the group II decarboxylase family. | 0.902 |
Acnat2 | Gad2 | ENSMUSP00000080256 | ENSMUSP00000028123 | Acyl-coenzyme A amino acid N-acyltransferase 2; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine (By similarity). | Glutamate decarboxylase 2; Catalyzes the production of GABA. | 0.902 |
Acnat2 | Ggt1 | ENSMUSP00000080256 | ENSMUSP00000006508 | Acyl-coenzyme A amino acid N-acyltransferase 2; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine (By similarity). | Glutathione hydrolase 1 heavy chain; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione [...] | 0.900 |
Acnat2 | Ggt6 | ENSMUSP00000080256 | ENSMUSP00000075773 | Acyl-coenzyme A amino acid N-acyltransferase 2; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine (By similarity). | Glutathione hydrolase 6 heavy chain; Cleaves glutathione conjugates; Belongs to the gamma-glutamyltransferase family. | 0.908 |
Acnat2 | Scp2 | ENSMUSP00000080256 | ENSMUSP00000030340 | Acyl-coenzyme A amino acid N-acyltransferase 2; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine (By similarity). | Non-specific lipid-transfer protein; Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis. | 0.936 |
Acnat2 | Slc27a5 | ENSMUSP00000080256 | ENSMUSP00000032539 | Acyl-coenzyme A amino acid N-acyltransferase 2; Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine (By similarity). | Bile acyl-CoA synthetase; Acyl-CoA synthetase that catalyzes the activation of bile acids via formation of bile acid CoA thioesters which is necessary for their subsequent conjugation with glycine or taurine. Catalyzes the activation of the primary bile acid, cholic acid. Both primary bile acid (chenodeoxycholic acid) and secondary bile acids (deoxycholic acid and lithocholic acid) are the principal substrates (By similarity). Also exhibits acyl CoA synthetase activity that activates very long-chain fatty acids (VLCFAs) by catalyzing the formation of fatty acyl-CoA (By similarity). In [...] | 0.964 |