Lipase

Details

Name
Lipase
Synonyms
  • 3.1.1.3
  • Triacylglycerol lipase
Gene Name
lipA
Organism
Pseudomonas cepacia
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
Functions
metal ion binding / triglyceride lipase activity
Processes
lipid catabolic process
General Function
Triglyceride lipase activity
Specific Function
Catalyzes the hydrolysis of triglycerides.
Pfam Domain Function
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
ResourceLink
UniProtKB IDP22088
UniProtKB Entry NameLIP_BURCE
GenBank Protein ID557867
GenBank Gene IDM58494
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB06965Hexylphosphonic acid (R)-2-methyl-3-phenylpropyl esterexperimentalunknownDetails
DB06966Hexylphosphonic acid (S)-2-methyl-3-phenylpropyl esterexperimentalunknownDetails
DB07990(RP,SP)-O-(2R)-(1-PHENOXYBUT-2-YL)-METHYLPHOSPHONIC ACID CHLORIDEexperimentalunknownDetails
DB08419(1S)-1-(PHENOXYMETHYL)PROPYL METHYLPHOSPHONOCHLORIDOATEexperimentalunknownDetails