node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ALDH1A1 | BCMO1 | ENSP00000297785 | ENSP00000258168 | aldehyde dehydrogenase 1 family, member A1; Binds free retinal and cellular retinol-binding protein- bound retinal. Can convert/oxidize retinaldehyde to retinoic acid (By similarity) | beta-carotene 15,15’-monooxygenase 1; Symmetrically cleaves beta-carotene into two molecules of retinal. The reaction proceeds in three stages, epoxidation of the 15,15’-double bond, hydration of the double bond leading to ring opening, and oxidative cleavage of the diol formed | 0.925 |
ALDH1A1 | CYP26A1 | ENSP00000297785 | ENSP00000224356 | aldehyde dehydrogenase 1 family, member A1; Binds free retinal and cellular retinol-binding protein- bound retinal. Can convert/oxidize retinaldehyde to retinoic acid (By similarity) | cytochrome P450, family 26, subfamily A, polypeptide 1; Plays a key role in retinoic acid metabolism. Acts on retinoids, including all-trans-retinoic acid (RA) and its stereoisomer 9-cis-RA. Capable of both 4-hydroxylation and 18- hydroxylation. Responsible for generation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA | 0.963 |
ALDH1A1 | CYP26B1 | ENSP00000297785 | ENSP00000001146 | aldehyde dehydrogenase 1 family, member A1; Binds free retinal and cellular retinol-binding protein- bound retinal. Can convert/oxidize retinaldehyde to retinoic acid (By similarity) | cytochrome P450, family 26, subfamily B, polypeptide 1 | 0.957 |
ALDH1A1 | RDH16 | ENSP00000297785 | ENSP00000381206 | aldehyde dehydrogenase 1 family, member A1; Binds free retinal and cellular retinol-binding protein- bound retinal. Can convert/oxidize retinaldehyde to retinoic acid (By similarity) | retinol dehydrogenase 16 (all-trans); Oxidoreductase with a preference for NAD. Oxidizes all- trans-retinol and 13-cis-retinol to the corresponding aldehydes. Has higher activity towards CRBP-bound retinol than with free retinol. Oxidizes 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction | 0.913 |
ALDH1A2 | BCMO1 | ENSP00000249750 | ENSP00000258168 | aldehyde dehydrogenase 1 family, member A2; Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Does metabolize octanal and decanal but does not metabolize citral, benzaldehyde, acetaldehyde and propanal efficiently (By similarity) | beta-carotene 15,15’-monooxygenase 1; Symmetrically cleaves beta-carotene into two molecules of retinal. The reaction proceeds in three stages, epoxidation of the 15,15’-double bond, hydration of the double bond leading to ring opening, and oxidative cleavage of the diol formed | 0.923 |
ALDH1A2 | CYP26A1 | ENSP00000249750 | ENSP00000224356 | aldehyde dehydrogenase 1 family, member A2; Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Does metabolize octanal and decanal but does not metabolize citral, benzaldehyde, acetaldehyde and propanal efficiently (By similarity) | cytochrome P450, family 26, subfamily A, polypeptide 1; Plays a key role in retinoic acid metabolism. Acts on retinoids, including all-trans-retinoic acid (RA) and its stereoisomer 9-cis-RA. Capable of both 4-hydroxylation and 18- hydroxylation. Responsible for generation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA | 0.982 |
ALDH1A2 | CYP26B1 | ENSP00000249750 | ENSP00000001146 | aldehyde dehydrogenase 1 family, member A2; Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Does metabolize octanal and decanal but does not metabolize citral, benzaldehyde, acetaldehyde and propanal efficiently (By similarity) | cytochrome P450, family 26, subfamily B, polypeptide 1 | 0.971 |
ALDH1A2 | RDH16 | ENSP00000249750 | ENSP00000381206 | aldehyde dehydrogenase 1 family, member A2; Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Does metabolize octanal and decanal but does not metabolize citral, benzaldehyde, acetaldehyde and propanal efficiently (By similarity) | retinol dehydrogenase 16 (all-trans); Oxidoreductase with a preference for NAD. Oxidizes all- trans-retinol and 13-cis-retinol to the corresponding aldehydes. Has higher activity towards CRBP-bound retinol than with free retinol. Oxidizes 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction | 0.926 |
AOX1 | BCMO1 | ENSP00000363832 | ENSP00000258168 | aldehyde oxidase 1 | beta-carotene 15,15’-monooxygenase 1; Symmetrically cleaves beta-carotene into two molecules of retinal. The reaction proceeds in three stages, epoxidation of the 15,15’-double bond, hydration of the double bond leading to ring opening, and oxidative cleavage of the diol formed | 0.906 |
AOX1 | CYP26A1 | ENSP00000363832 | ENSP00000224356 | aldehyde oxidase 1 | cytochrome P450, family 26, subfamily A, polypeptide 1; Plays a key role in retinoic acid metabolism. Acts on retinoids, including all-trans-retinoic acid (RA) and its stereoisomer 9-cis-RA. Capable of both 4-hydroxylation and 18- hydroxylation. Responsible for generation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA | 0.906 |
AOX1 | CYP26B1 | ENSP00000363832 | ENSP00000001146 | aldehyde oxidase 1 | cytochrome P450, family 26, subfamily B, polypeptide 1 | 0.912 |
AOX1 | RDH16 | ENSP00000363832 | ENSP00000381206 | aldehyde oxidase 1 | retinol dehydrogenase 16 (all-trans); Oxidoreductase with a preference for NAD. Oxidizes all- trans-retinol and 13-cis-retinol to the corresponding aldehydes. Has higher activity towards CRBP-bound retinol than with free retinol. Oxidizes 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction | 0.900 |
AWAT2 | CYP26A1 | ENSP00000421172 | ENSP00000224356 | acyl-CoA wax alcohol acyltransferase 2; Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has no activity using decyl alcohol and significantly prefers the C16 and C18 alcohols. May also have 2-acylglycerol O-acyltransferase (MGAT) and acyl- CoA-retinol acyltransferase (ARAT) activities, to catalyze the synthesis of diacylglycerols and retinyl esters; however this activity is unclear in vivo | cytochrome P450, family 26, subfamily A, polypeptide 1; Plays a key role in retinoic acid metabolism. Acts on retinoids, including all-trans-retinoic acid (RA) and its stereoisomer 9-cis-RA. Capable of both 4-hydroxylation and 18- hydroxylation. Responsible for generation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA | 0.905 |
AWAT2 | RDH16 | ENSP00000421172 | ENSP00000381206 | acyl-CoA wax alcohol acyltransferase 2; Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has no activity using decyl alcohol and significantly prefers the C16 and C18 alcohols. May also have 2-acylglycerol O-acyltransferase (MGAT) and acyl- CoA-retinol acyltransferase (ARAT) activities, to catalyze the synthesis of diacylglycerols and retinyl esters; however this activity is unclear in vivo | retinol dehydrogenase 16 (all-trans); Oxidoreductase with a preference for NAD. Oxidizes all- trans-retinol and 13-cis-retinol to the corresponding aldehydes. Has higher activity towards CRBP-bound retinol than with free retinol. Oxidizes 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction | 0.900 |
AWAT2 | RETSAT | ENSP00000421172 | ENSP00000295802 | acyl-CoA wax alcohol acyltransferase 2; Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has no activity using decyl alcohol and significantly prefers the C16 and C18 alcohols. May also have 2-acylglycerol O-acyltransferase (MGAT) and acyl- CoA-retinol acyltransferase (ARAT) activities, to catalyze the synthesis of diacylglycerols and retinyl esters; however this activity is unclear in vivo | retinol saturase (all-trans-retinol 13,14-reductase); Retinol saturase carrying out the saturation of the 13- 14 double bond of all-trans-retinol to produce all-trans-13,14- dihydroretinol. Has activity toward all-trans-retinol as substrate. Does not use all-trans-retinoic acid nor 9-cis, 11-cis or 13-cis-retinol isomers as substrates. May play a role in the metabolism of vitamin A (By similarity) | 0.900 |
AWAT2 | SQLE | ENSP00000421172 | ENSP00000265896 | acyl-CoA wax alcohol acyltransferase 2; Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has no activity using decyl alcohol and significantly prefers the C16 and C18 alcohols. May also have 2-acylglycerol O-acyltransferase (MGAT) and acyl- CoA-retinol acyltransferase (ARAT) activities, to catalyze the synthesis of diacylglycerols and retinyl esters; however this activity is unclear in vivo | squalene epoxidase; Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway | 0.485 |
BCMO1 | ALDH1A1 | ENSP00000258168 | ENSP00000297785 | beta-carotene 15,15’-monooxygenase 1; Symmetrically cleaves beta-carotene into two molecules of retinal. The reaction proceeds in three stages, epoxidation of the 15,15’-double bond, hydration of the double bond leading to ring opening, and oxidative cleavage of the diol formed | aldehyde dehydrogenase 1 family, member A1; Binds free retinal and cellular retinol-binding protein- bound retinal. Can convert/oxidize retinaldehyde to retinoic acid (By similarity) | 0.925 |
BCMO1 | ALDH1A2 | ENSP00000258168 | ENSP00000249750 | beta-carotene 15,15’-monooxygenase 1; Symmetrically cleaves beta-carotene into two molecules of retinal. The reaction proceeds in three stages, epoxidation of the 15,15’-double bond, hydration of the double bond leading to ring opening, and oxidative cleavage of the diol formed | aldehyde dehydrogenase 1 family, member A2; Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Does metabolize octanal and decanal but does not metabolize citral, benzaldehyde, acetaldehyde and propanal efficiently (By similarity) | 0.923 |
BCMO1 | AOX1 | ENSP00000258168 | ENSP00000363832 | beta-carotene 15,15’-monooxygenase 1; Symmetrically cleaves beta-carotene into two molecules of retinal. The reaction proceeds in three stages, epoxidation of the 15,15’-double bond, hydration of the double bond leading to ring opening, and oxidative cleavage of the diol formed | aldehyde oxidase 1 | 0.906 |
BCMO1 | RDH16 | ENSP00000258168 | ENSP00000381206 | beta-carotene 15,15’-monooxygenase 1; Symmetrically cleaves beta-carotene into two molecules of retinal. The reaction proceeds in three stages, epoxidation of the 15,15’-double bond, hydration of the double bond leading to ring opening, and oxidative cleavage of the diol formed | retinol dehydrogenase 16 (all-trans); Oxidoreductase with a preference for NAD. Oxidizes all- trans-retinol and 13-cis-retinol to the corresponding aldehydes. Has higher activity towards CRBP-bound retinol than with free retinol. Oxidizes 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction | 0.912 |