IED Industry Enzyme Database

Detail Information for IndEnz0010001530
IED ID IndEnz0010001530
Enzyme Type ID esterase001530
Protein Name Phospholipase B1, membrane-associated
Phospholipase B
hPLB
Lysophospholipase
EC 3.1.1.5
Phospholipase A2
EC 3.1.1.4
Phospholipase B/lipase
PLB/LIP
Triacylglycerol lipase
EC 3.1.1.3
Gene Name PLB1 PLB
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MGLRPGIFLLELLLLLGQGTPQIHTSPRKSTLEGQLWPETLKNSPFPCNPNKLGVNMPSKSVHSLKPSDIKFVAAIGNLEIPPDPGTGDLEKQDWTERPQQVCMGVMTVLSDIIRYFSPSVPMPVCHTGKRVIPHDGAEDLWIQAQELVRNMKENLQLDFQFDWKLINVFFSNASQCYLCPSAQQNGLAAGGVDELMGVLDYLQQEVPRAFVNLVDLSEVAEVSRQYHGTWLSPAPEPCNCSEETTRLAKVVMQWSYQEAWNSLLASSRYSEQESFTVVFQPFFYETTPSLHSEDPRLQDSTTLAWHLWNRMMEPAGEKDEPLSVKHGRPMKCPSQESPYLFSYRNSNYLTRLQKPQDKLEVREGAEIRCPDKDPSDTVPTSVHRLKPADINVIGALGDSLTAGNGAGSTPGNVLDVLTQYRGLSWSVGGDENIGTVTTLANILREFNPSLKGFSVGTGKETSPNAFLNQAVAGGRAEDLPVQARRLVDLMKNDTRIHFQEDWKIITLFIGGNDLCDFCNDLVHYSPQNFTDNIGKALDILHAEVPRAFVNLVTVLEIVNLRELYQEKKVYCPRMILRSLCPCVLKFDDNSTELATLIEFNKKFQEKTHQLIESGRYDTREDFTVVVQPFFENVDMPKTSEGLPDNSFFAPDCFHFSSKSHSRAASALWNNMLEPVGQKTTRHKFENKINITCPNQVQPFLRTYKNSMQGHGTWLPCRDRAPSALHPTSVHALRPADIQVVAALGDSLTAGNGIGSKPDDLPDVTTQYRGLSYSAGGDGSLENVTTLPNILREFNRNLTGYAVGTGDANDTNAFLNQAVPGAKAEDLMSQVQTLMQKMKDDHRVNFHEDWKVITVLIGGSDLCDYCTDSNLYSAANFVHHLRNALDVLHREVPRVLVNLVDFLNPTIMRQVFLGNPDKCPVQQASVLCNCVLTLRENSQELARLEAFSRAYRSSMRELVGSGRYDTQEDFSVVLQPFFQNIQLPVLADGLPDTSFFAPDCIHPNQKFHSQLARALWTNMLEPLGSKTETLDLRAEMPITCPTQNEPFLRTPRNSNYTYPIKPAIENWGSDFLCTEWKASNSVPTSVHQLRPADIKVVAALGDSLTTAVGARPNNSSDLPTSWRGLSWSIGGDGNLETHTTLPNILKKFNPYLLGFSTSTWEGTAGLNVAAEGARARDMPAQAWDLVERMKNSPDINLEKDWKLVTLFIGVNDLCHYCENPEAHLATEYVQHIQQALDILSEELPRAFVNVVEVMELASLYQGQGGKCAMLAAQNNCTCLRHSQSSLEKQELKKVNWNLQHGISSFSYWHQYTQREDFAVVVQPFFQNTLTPLNERGDTDLTFFSEDCFHFSDRGHAEMAIALWNNMLEPVGRKTTSNNFTHSRAKLKCPSPESPYLYTLRNSRLLPDQAEEAPEVLYWAVPVAAGVGLVVGIIGTVVWRCRRGGRREDPPMSLRTVAL
Enzyme Length 1458
Uniprot Accession Number Q6P1J6
Absorption
Active Site ACT_SITE 400; /evidence=ECO:0000250|UniProtKB:O54728; ACT_SITE 514; /evidence=ECO:0000250|UniProtKB:O54728; ACT_SITE 655; /evidence=ECO:0000250|UniProtKB:O54728
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40923, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40924; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; Evidence={ECO:0000250|UniProtKB:Q05017};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; Evidence={ECO:0000250|UniProtKB:Q05017}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:40971, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73002, ChEBI:CHEBI:76084; Evidence={ECO:0000250|UniProtKB:Q05017};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40972; Evidence={ECO:0000250|UniProtKB:Q05017}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40911, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:73004, ChEBI:CHEBI:73007; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72841, ChEBI:CHEBI:75158; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + 2 H2O = 2 H(+) + 2 hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40975, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:Q05017};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40976; Evidence={ECO:0000250|UniProtKB:Q05017}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40915, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:34112, ChEBI:CHEBI:64496; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40916; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + H(+) + octadecanoate; Xref=Rhea:RHEA:41111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75466, ChEBI:CHEBI:77623; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41112; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = (9Z)-octadecenoate + 1,3-dihexadecanoylglycerol + H(+); Xref=Rhea:RHEA:40983, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75688, ChEBI:CHEBI:77619; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40984; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:40979, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75585, ChEBI:CHEBI:75688; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40980; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-3-octadecanoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:41103, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77623, ChEBI:CHEBI:77624; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41104; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = 2-(9Z-octadecenoyl)-3-octadecanoyl-sn-glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:41107, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75558, ChEBI:CHEBI:77623; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41108; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + H2O = (9Z,12Z)-octadecadienoate + 1-octadecanoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:40927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:75550, ChEBI:CHEBI:77097; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40928; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:41219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:75757; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41220; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=2,3-di-(9Z)-octadecenoyl-sn-glycerol + H2O = (9Z)-octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:42604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75824, ChEBI:CHEBI:75938; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42605; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:39939, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75735, ChEBI:CHEBI:75937; Evidence={ECO:0000250|UniProtKB:Q05017};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39940; Evidence={ECO:0000250|UniProtKB:Q05017}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q05017};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000250|UniProtKB:Q05017}; CATALYTIC ACTIVITY: Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:Q05017};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492; Evidence={ECO:0000250|UniProtKB:Q05017};
DNA Binding
EC Number 3.1.1.5; 3.1.1.4; 3.1.1.3
Enzyme Function FUNCTION: Calcium-independent membrane-associated phospholipase that catalyzes complete diacylation of phospholipids by hydrolyzing both sn-1 and sn-2 fatty acyl chains attached to the glycerol backbone (phospholipase B activity) (By similarity). Has dual phospholipase and lysophospholipase activities toward diacylphospholipids. Preferentially cleaves sn-2 ester bonds over sn-1 bonds. Acts as a lipase toward glycerolipid substrates (By similarity). Hydrolyzes fatty acyl chains of diacylglycerols with preference for the sn-2 position and of triacylglycerols with not positional selectivity (By similarity). May also hydrolyze long chain retinyl esters such as retinyl palmitate (By similarity). May contribute to digestion of dietary phospholipids, glycerolipids and retinoids, facilitating lipid absorption at the brush border (By similarity). {ECO:0000250|UniProtKB:O54728, ECO:0000250|UniProtKB:Q05017}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (8); Chain (1); Erroneous initiation (1); Glycosylation (13); Natural variant (6); Region (2); Repeat (4); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1)
Keywords Alternative splicing;Cell membrane;Glycoprotein;Hydrolase;Lipid metabolism;Membrane;Phospholipid metabolism;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix
Interact With O43559; P14136; Q5SUL5; O75031; Q8WXH2; Q92993; O14901; Q8TAP4-4; Q13449; P19404; P17252; Q15047-2; Q8WW01; P61981
Induction
Subcellular Location SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:O54728}; Single-pass type I membrane protein {ECO:0000255}. Note=Present in the intestinal brush border membranes. {ECO:0000250|UniProtKB:O54728}.
Modified Residue
Post Translational Modification PTM: Undergoes proteolytic cleavage in the ileum. {ECO:0000250|UniProtKB:O54728}.
Signal Peptide SIGNAL 1..21; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 1618844; 24520335; 28104536; 8017323;
Motif
Gene Encoded By
Mass 163,081
Kinetics
Metal Binding
Rhea ID RHEA:15801; RHEA:15802; RHEA:15177; RHEA:15178; RHEA:12044; RHEA:12045; RHEA:41223; RHEA:41224; RHEA:38779; RHEA:38780; RHEA:40923; RHEA:40924; RHEA:40811; RHEA:40812; RHEA:40971; RHEA:40972; RHEA:40911; RHEA:40912; RHEA:40919; RHEA:40920; RHEA:40975; RHEA:40976; RHEA:40915; RHEA:40916; RHEA:40435; RHEA:40436; RHEA:38575; RHEA:38576; RHEA:41111; RHEA:41112; RHEA:40983; RHEA:40984; RHEA:40979; RHEA:40980; RHEA:41103; RHEA:41104; RHEA:41107; RHEA:41108; RHEA:40927; RHEA:40928; RHEA:41219; RHEA:41220; RHEA:42604; RHEA:42605; RHEA:39939; RHEA:39940; RHEA:38487; RHEA:38488; RHEA:38491; RHEA:38492
Cross Reference Brenda