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 | 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 | 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 | Ggt5 | ENSMUSP00000092702 | ENSMUSP00000072074 | 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 5 heavy chain; Cleaves the gamma-glutamyl peptide bond of glutathione conjugates, but maybe not glutathione itself. Converts leukotriene C4 (LTC4) to leukotriene D4 (LTD4). | 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 | Ggt7 | ENSMUSP00000092702 | ENSMUSP00000029131 | 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 7 heavy chain; Cleaves glutathione conjugates. | 0.900 |
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 | Agxt2 | ENSMUSP00000080256 | ENSMUSP00000022858 | 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). | Alanine--glyoxylate aminotransferase 2, mitochondrial; Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure. | 0.561 |
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 | 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 | Ggt5 | ENSMUSP00000080256 | ENSMUSP00000072074 | 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 5 heavy chain; Cleaves the gamma-glutamyl peptide bond of glutathione conjugates, but maybe not glutathione itself. Converts leukotriene C4 (LTC4) to leukotriene D4 (LTD4). | 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 | Ggt7 | ENSMUSP00000080256 | ENSMUSP00000029131 | 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 7 heavy chain; Cleaves glutathione conjugates. | 0.900 |
Ado | Cdo1 | ENSMUSP00000075107 | ENSMUSP00000046517 | 2-aminoethanethiol dioxygenase. | Cysteine dioxygenase type 1; Belongs to the cysteine dioxygenase family. | 0.866 |
Ado | Csad | ENSMUSP00000075107 | ENSMUSP00000023805 | 2-aminoethanethiol dioxygenase. | 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. | 0.967 |
Agxt2 | Acnat2 | ENSMUSP00000022858 | ENSMUSP00000080256 | Alanine--glyoxylate aminotransferase 2, mitochondrial; Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure. | 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). | 0.561 |
Agxt2 | Csad | ENSMUSP00000022858 | ENSMUSP00000023805 | Alanine--glyoxylate aminotransferase 2, mitochondrial; Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure. | 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. | 0.922 |
Baat | Acnat1 | ENSMUSP00000041983 | ENSMUSP00000092702 | 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 [...] | 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. | 0.908 |