Lipase
Details
- Name
- Lipase
- Kind
- protein
- Synonyms
- 3.1.1.3
- Triacylglycerol lipase
- Gene Name
- lipA
- UniProtKB Entry
- P22088Swiss-Prot
- Organism
- Pseudomonas cepacia
- NCBI Taxonomy ID
- 292
- Amino acid sequence
>lcl|BSEQ0017218|Lipase MARTMRSRVVAGAVACAMSIAPFAGTTAVMTLATTHAAMAATAPAAGYAATRYPIILVHG LSGTDKYAGVLEYWYGIQEDLQQNGATVYVANLSGFQSDDGPNGRGEQLLAYVKTVLAAT GATKVNLVGHSQGGLSSRYVAAVAPDLVASVTTIGTPHRGSEFADFVQDVLAYDPTGLSS SVIAAFVNVFGILTSSSHNTNQDALAALQTLTTARAATYNQNYPSAGLGAPGSCQTGAPT ETVGGNTHLLYSWAGTAIQPTLSVFGVTGATDTSTLPLVDPANVLDLSTLALFGTGTVMI NRGSGQNDGLVSKCSALYGKVLSTSYKWNHLDEINQLLGVRGAYAEDPVAVIRTHANRLK LAGV
- Number of residues
- 364
- Molecular Weight
- 37493.945
- Theoretical pI
- 6.71
- GO Classification
- Functionsmetal ion binding / triglyceride lipase activityProcesseslipid catabolic process
- General Function
- Catalyzes the hydrolysis of triacylglycerol. It shows a preference for triacylglycerols with a chain length between 6 and 12 carbons.
- Specific Function
- metal ion binding
- Pfam Domain Function
- Abhydrolase_1 (PF00561)
- Signal Regions
- 1-44
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0007223|1095 bp ATGGCCAGGACGATGCGTTCCAGGGTGGTGGCAGGGGCAGTGGCATGCGCGATGAGCATC GCGCCGTTCGCGGGGACGACCGCGGTGATGACGCTCGCGACGACGCACGCGGCAATGGCG GCCACCGCGCCCGCCGCTGGCTACGCGGCGACGCGTTACCCGATCATCCTCGTGCACGGG CTCTCGGGTACCGACAAGTACGCCGGCGTGCTCGAGTATTGGTACGGCATCCAGGAGGAC CTGCAACAGAACGGTGCGACCGTCTACGTCGCGAACCTGTCGGGTTTCCAGAGCGACGAC GGCCCGAACGGGCGCGGCGAACAGTTGCTCGCTTACGTGAAGACGGTGCTCGCGGCGACG GGGGCGACCAAGGTCAATCTCGTCGGTCACAGCCAGGGCGGCCTCTCGTCGCGCTATGTT GCTGCCGTCGCGCCCGATCTCGTTGCGTCGGTGACGACGATCGGCACGCCGCATCGCGGC TCCGAATTCGCCGACTTCGTGCAGGACGTGCTCGCGTACGATCCGACCGGGCTTTCGTCA TCGGTGATCGCCGCGTTCGTCAATGTGTTCGGGATCCTGACGAGCAGCAGCCACAACACC AACCAGGACGCGCTCGCCGCACTGCAGACGCTGACCACCGCACGGGCCGCCACGTACAAC CAGAACTATCCGAGCGCGGGCCTGGGTGCGCCGGGCAGTTGCCAGACCGGTGCGCCGACC GAAACCGTCGGCGGCAACACGCACCTGCTGTATTCGTGGGCCGGCACGGCGATCCAGCCG ACGCTCTCCGTGTTCGGCGTCACGGGCGCGACGGACACGAGCACCCTTCCGCTCGTCGAT CCGGCGAACGTGCTCGACCTGTCGACGCTCGCGCTGTTCGGCACCGGCACGGTGATGATC AACCGCGGCTCCGGGCAGAACGACGGGCTCGTGTCGAAGTGCAGTGCGCTGTACGGCAAG GTGCTGAGCACGAGCTACAAGTGGAACCACCTCGACGAGATCAACCAGCTGCTCGGCGTG CGCGGCGCGTATGCGGAAGATCCCGTCGCGGTGATCCGCACGCATGCGAACCGGCTGAAG CTGGCGGGCGTGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P22088 UniProtKB Entry Name LIP_BURCE GenBank Protein ID 557867 GenBank Gene ID M58494 PDB ID(s) 1HQD, 1OIL, 1YS1, 1YS2, 2LIP, 2NW6, 3LIP, 4LIP, 5LIP - General References
- Jorgensen S, Skov KW, Diderichsen B: Cloning, sequence, and expression of a lipase gene from Pseudomonas cepacia: lipase production in heterologous hosts requires two Pseudomonas genes. J Bacteriol. 1991 Jan;173(2):559-67. [Article]
- Kim KK, Song HK, Shin DH, Hwang KY, Suh SW: The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor. Structure. 1997 Feb 15;5(2):173-85. [Article]
- Schrag JD, Li Y, Cygler M, Lang D, Burgdorf T, Hecht HJ, Schmid R, Schomburg D, Rydel TJ, Oliver JD, Strickland LC, Dunaway CM, Larson SB, Day J, McPherson A: The open conformation of a Pseudomonas lipase. Structure. 1997 Feb 15;5(2):187-202. [Article]
- Lang DA, Mannesse ML, de Haas GH, Verheij HM, Dijkstra BW: Structural basis of the chiral selectivity of Pseudomonas cepacia lipase. Eur J Biochem. 1998 Jun 1;254(2):333-40. [Article]
- Luic M, Tomic S, Lescic I, Ljubovic E, Sepac D, Sunjic V, Vitale L, Saenger W, Kojic-Prodic B: Complex of Burkholderia cepacia lipase with transition state analogue of 1-phenoxy-2-acetoxybutane: biocatalytic, structural and modelling study. Eur J Biochem. 2001 Jul;268(14):3964-73. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Hexylphosphonic acid (R)-2-methyl-3-phenylpropyl ester experimental unknown target Details Hexylphosphonic acid (S)-2-methyl-3-phenylpropyl ester experimental unknown target Details (RP,SP)-O-(2R)-(1-PHENOXYBUT-2-YL)-METHYLPHOSPHONIC ACID CHLORIDE experimental unknown target Details (1S)-1-(PHENOXYMETHYL)PROPYL METHYLPHOSPHONOCHLORIDOATE experimental unknown target Details