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Identification
NameLysophospholipase 2
Synonyms
  • Phospholipase B 2
Gene NamePLB2
Enzyme Class
Biological Properties
General FunctionInvolved in metabolic process
Specific FunctionSequentially removes both fatty acyl groups from diacylglycerophospholipids and therefore has both phospholipase A and lysophospholipase activities. Substrate preference is phosphatidylserine > phosphatidylinositol > phosphatidylcholine > phosphatidylethanolamine
Cellular LocationSecreted, cell wall. Membrane; Lipid-anchor, GPI-anchor.
SMPDB Pathways
Glycerophospholipid metabolismPW002493 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Glycerophospholipid metabolismec00564 Map00564
SMPDB ReactionsNot Available
KEGG Reactions
hydron + Glycerophosphocholine + fatty acid ↔ 1-O-acylglycerophosphocholine + water
Metabolites
YMDB IDNameView
YMDB00309GlycerophosphocholineShow
YMDB00694sn-Glycero-3-phosphocholineShow
YMDB00862hydronShow
YMDB00890waterShow
GO Classification
Component
Not Available
Function
hydrolase activity
hydrolase activity, acting on ester bonds
lipase activity
phospholipase activity
catalytic activity
Process
organophosphate metabolic process
phospholipid metabolic process
phospholipid catabolic process
metabolic process
Gene Properties
Chromosome Locationchromosome 13
LocusYMR006C
Gene Sequence>2121 bp ATGCAATTACGGAACATATTACAGGCTAGCTCGCTAATTTCTGGACTTTCGCTCGCTGCA GATTCGTCGTCCACTACTGGTGATGGTTATGCTCCATCAATAATTCCTTGTCCCAGTGAT GATACCTCTTTAGTTAGAAACGCGTCTGGCTTATCTACCGCTGAAACTGATTGGTTAAAG AAAAGAGATGCGTACACTAAAGAAGCTTTACATTCCTTCTTAAGCAGAGCTACTTCTAAC TTCAGTGACACTTCTTTGCTATCCACTCTTTTCAGTAGTAACTCTTCCAATGTACCCAAA ATTGGTATTGCATGCTCTGGTGGTGGTTATCGTGCCATGTTGGGTGGTGCTGGTATGATT GCTGCTATGGACAATCGTACTGATGGTGCTAACGAGCATGGTCTTGGTGGTTTACTACAA AGTTCCACGTATCTATCGGGTTTGTCCGGTGGTAACTGGTTGACTGGTACTTTGGCATGG AACAATTGGACCTCTGTACAGGAAATTGTAGACCATATGAGTGAGAGCGATTCCATCTGG AATATCACGAAATCCATTGTGAACCCTGGTGGCTCTAATTTGACCTACACAATTGAAAGA TGGGAGTCCATTGTACAAGAAGTGCAGGCTAAGTCTGATGCAGGCTTCAATATATCTTTG TCGGATTTGTGGGCCCGTGCACTTTCTTACAACTTCTTTCCAAGCTTGCCAGATGCTGGC TCCGCTTTGACTTGGTCCTCTTTGAGAGATGTTGATGTGTTCAAAAACGGTGAAATGCCT TTACCAATTACTGTTGCAGATGGTAGATACCCAGGTACCACCGTGATAAACTTGAATGCC ACTCTTTTCGAGTTCACTCCATTTGAAATGGGTTCTTGGGATCCTTCTTTGAACGCTTTT ACGGATGTGAAATATCTAGGTACCAACGTTACAAATGGTAAACCGGTCAACAAGGATCAA TGCGTTTCTGGTTACGATAATGCTGGATTTGTAATTGCCACATCCGCCAGTTTATTCAAC GAATTTTCCCTGGAAGCTTCCACTTCGACCTATTATAAAATGATTAATAGTTTTGCCAAC AAGTACGTTAACAACCTATCCCAAGATGACGATGATATTGCAATTTACGCTGCAAATCCA TTCAAGGATACAGAATTTGTTGACCGCAATTACACTTCCAGTATTGTTGATGCCGATGAT TTGTTTTTAGTTGATGGTGGTGAGGACGGCCAAAATTTGCCGTTGGTTCCACTAATCAAG AAGGAACGTGACTTGGATGTGGTGTTCGCATTGGATATATCCGACAATACTGATGAATCA TGGCCAAGTGGTGTGTGCATGACGAACACTTATGAGCGCCAGTATTCTAAGCAAGGTAAA GGAATGGCTTTCCCATATGTTCCAGACGTTAACACCTTCCTTAACTTGGGCTTAACTAAT AAGCCAACGTTTTTTGGTTGTGATGCAAAAAATTTGACGGACTTGGAGTATATTCCACCT TTAGTTGTATATATCCCAAACACAAAACATTCATTCAATGGTAACCAAAGTACTTTGAAG ATGAACTACAATGTTACAGAACGTCTTGGAATGATCAGAAATGGTTTTGAAGCTGCTACA ATGGGCAACTTTACGGATGACTCTAACTTTTTAGGTTGCATAGGTTGTGCCATCATTAGA CGTAAGCAAGAAAGCCTAAATGCCACCTTGCCCCCTGAATGTACCAAATGTTTTGCGGAT TACTGCTGGAACGGCACACTAAGTACCTCAGCTAATCCTGAACTATCGGGAAATAGTACG TATCAAAGCGGTGCTATTGCCTCTGCAATCTCTGAGGCTACTGACGGTATTCCAATAACG GCTCTCTTAGGTTCATCAACCTCCGGAAATACTACATCAAACTCAACAACCTCGACTTCA TCAAATGTCACTTCTAACTCAAACTCTTCGTCAAATACAACTTTAAACTCAAATTCTTCA TCCTCTTCAATTTCTTCCTCTACAGCTCGTTCTTCTTCCTCTACGGCAAACAAAGCGAAT GCTGCGGCTATTTCCTATGCGAACACTAATACTCTAATGAGTTTGTTAGGTGCCATAACA GCATTATTTGGACTAATTTAG
Protein Properties
Pfam Domain Function
Protein Residues706
Protein Molecular Weight75454.60156
Protein Theoretical pI4.28
Signalling Regions
  • 1-19
Transmembrane Regions
  • None
Protein Sequence>Lysophospholipase 2 MQLRNILQASSLISGLSLAADSSSTTGDGYAPSIIPCPSDDTSLVRNASGLSTAETDWLK KRDAYTKEALHSFLSRATSNFSDTSLLSTLFSSNSSNVPKIGIACSGGGYRAMLGGAGMI AAMDNRTDGANEHGLGGLLQSSTYLSGLSGGNWLTGTLAWNNWTSVQEIVDHMSESDSIW NITKSIVNPGGSNLTYTIERWESIVQEVQAKSDAGFNISLSDLWARALSYNFFPSLPDAG SALTWSSLRDVDVFKNGEMPLPITVADGRYPGTTVINLNATLFEFTPFEMGSWDPSLNAF TDVKYLGTNVTNGKPVNKDQCVSGYDNAGFVIATSASLFNEFSLEASTSTYYKMINSFAN KYVNNLSQDDDDIAIYAANPFKDTEFVDRNYTSSIVDADDLFLVDGGEDGQNLPLVPLIK KERDLDVVFALDISDNTDESWPSGVCMTNTYERQYSKQGKGMAFPYVPDVNTFLNLGLTN KPTFFGCDAKNLTDLEYIPPLVVYIPNTKHSFNGNQSTLKMNYNVTERLGMIRNGFEAAT MGNFTDDSNFLGCIGCAIIRRKQESLNATLPPECTKCFADYCWNGTLSTSANPELSGNST YQSGAIASAISEATDGIPITALLGSSTSGNTTSNSTTSTSSNVTSNSNSSSNTTLNSNSS SSSISSSTARSSSSTANKANAAAISYANTNTLMSLLGAITALFGLI
References
External Links
ResourceLink
Saccharomyces Genome Database PLB2
Uniprot IDQ03674
Uniprot NamePLB2_YEAST
GenBank Gene IDAF129165
Genebank Protein ID4732121
General Reference
  • Fyrst, H., Oskouian, B., Kuypers, F. A., Saba, J. D. (1999). "The PLB2 gene of Saccharomyces cerevisiae confers resistance to lysophosphatidylcholine and encodes a phospholipase B/lysophospholipase." Biochemistry 38:5864-5871.10231538
  • Bowman, S., Churcher, C., Badcock, K., Brown, D., Chillingworth, T., Connor, R., Dedman, K., Devlin, K., Gentles, S., Hamlin, N., Hunt, S., Jagels, K., Lye, G., Moule, S., Odell, C., Pearson, D., Rajandream, M., Rice, P., Skelton, J., Walsh, S., Whitehead, S., Barrell, B. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Nature 387:90-93.9169872
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Merkel, O., Fido, M., Mayr, J. A., Pruger, H., Raab, F., Zandonella, G., Kohlwein, S. D., Paltauf, F. (1999). "Characterization and function in vivo of two novel phospholipases B/lysophospholipases from Saccharomyces cerevisiae." J Biol Chem 274:28121-28127.10497163
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Yin, Q. Y., de Groot, P. W., Dekker, H. L., de Jong, L., Klis, F. M., de Koster, C. G. (2005). "Comprehensive proteomic analysis of Saccharomyces cerevisiae cell walls: identification of proteins covalently attached via glycosylphosphatidylinositol remnants or mild alkali-sensitive linkages." J Biol Chem 280:20894-20901.15781460