EzCatDB: D00143
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DB codeD00143
CATH domainDomain 11.20.90.10 : Phospholipase A2Catalytic domain
Domain 24.10.410.10 : Factor Xa Inhibitor
E.C.3.1.1.4


Enzyme Name
UniProtKBKEGG

P00617P00989
Protein namePhospholipase A2, beta bungarotoxin A1 chainBeta-bungarotoxin B2 chainphospholipase A2
lecithinase A
phosphatidase
phosphatidolipase
phospholipase A
SynonymsEC 3.1.1.4
Phosphatidylcholine 2-acylhydrolase
None
PfamPF00068 (Phospholip_A2_1)
[Graphical view]
PF00014 (Kunitz_BPTI)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00564Glycerophospholipid metabolism
MAP00565Ether lipid metabolism
MAP00590Arachidonic acid metabolism
MAP00591Linoleic acid metabolism
MAP00592alpha-Linolenic acid metabolism

UniProtKB:Accession NumberP00617P00989
Entry namePA21B_BUNMUIVB2_BUNMU
ActivityPhosphatidylcholine + H(2)O = 1- acylglycerophosphocholine + a carboxylate.
SubunitHeterodimer, disulfide-linked. The A chains have phospholipase A2 activity and the B chains show homology with the basic protease inhibitors. The A1 chain is found in beta-1 and beta-2 bungarotoxins.Heterodimer, disulfide-linked. The A chains have phospholipase A2 activity and the B chains show homology with the basic protease inhibitors.
Subcellular locationSecreted.Secreted.
CofactorBinds 1 calcium ion (By similarity).

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00076C00157C00001C00060C04230
CompoundCalciumphosphatidylcholineH2OCarboxylate1-Acyl-sn-glycero-3-phosphocholine
Typedivalent metal (Ca2+, Mg2+)amine group,carbohydrate,lipid,phosphate group/phosphate ionH2Ocarboxyl groupamine group,carbohydrate,lipid,phosphate group/phosphate ion
ChEBI29108

15377


PubChem271

962
22247451


             
1bunAAnalogue:_NA 87Unbound UnboundUnbound
1bunBUnboundUnbound UnboundUnbound

Active-site residues
resource
Swiss-prot;P00617
pdbCatalytic residuesCofactor-binding residues
          
1bunAHIS 48;ASP 94
TYR 28;GLY 30;GLY 32;ASP 49(Calcium binding)
1bunB 
 


references
[1]
CommentsCHARACTERIZATION OF PRESYNAPTIC NEUROTOXINS.
Medline ID78043174
PubMed ID303565
JournalEur J Biochem
Year1977
Volume80
Pages1-12
AuthorsAbe T, Alema S, Miledi R
TitleIsolation and characterization of presynaptically acting neurotoxins from the venom of Bungarus snakes.
Related UniProtKBP00617
[2]
CommentsCHARACTERIZATION OF PHOSPHOLIPASE A2 ACTIVITY.
Medline ID79088714
PubMed ID730754
JournalJ Biochem (Tokyo)
Year1978
Volume84
Pages1301-8
AuthorsKondo K, Toda H, Narita K
TitleCharacterization of phospholipase A activity of beta1-bungarotoxin from Bungarus multicinctus venom. II. Identification of the histidine residue of beta1-bungarotoxin modified by p-bromophenacyl bromide.
Related UniProtKBP00617
[3]
PubMed ID2590165
JournalBiochem J
Year1989
Volume262
Pages773-9
AuthorsChu ST, Chen YH
TitleThe intrinsic tryptophan fluorescence of beta 1-bungarotoxin and the Ca2+-binding domains of the toxin as probed with Tb3+ luminescence.
[4]
PubMed ID1898340
JournalBiochem J
Year1991
Volume278
Pages481-6
AuthorsChu ST, Chen YH
TitleRole of the N-terminal region of phospholipase A2 subunit of beta 1-bungarotoxin in the toxin-Ca2+ complex-formation.
[5]
PubMed ID1485347
JournalToxicon
Year1992
Volume30
Pages1501-4
AuthorsShina R, Rosenberg P, Condrea E
TitleAn EDTA.Ca2+ complex inhibits the enzymatic activity but not the lethality of beta-bungarotoxin.
[6]
PubMed ID8240282
JournalBiochem J
Year1993
Volume295
Pages713-8
AuthorsChu ST, Chu CC, Tseng CC, Chen YH
TitleMet-8 of the beta 1-bungarotoxin phospholipase A2 subunit is essential for the phospholipase A2-independent neurotoxic effect.
[7]
PubMed ID7702746
JournalJ Protein Chem
Year1994
Volume13
Pages641-8
AuthorsChang LS, Kuo KW, Lin SR, Chang CC
TitleFunctional involvement of Lys-6 in the enzymatic activity of phospholipase A2 from Bungarus multicinctus (Taiwan banded krait) snake venom.
[8]
PubMed ID8060495
JournalJ Protein Chem
Year1994
Volume13
Pages233-6
AuthorsChang LS, Lin SR, Chang CC, Yang CC
TitleThe essentiality of B chain in stabilizing the structure of the A chain in beta 1-bungarotoxin from Bungarus multicinctus venom.
[9]
CommentsX-ray crystallography
PubMed ID8590005
JournalStructure
Year1995
Volume3
Pages1109-19
AuthorsKwong PD, McDonald NQ, Sigler PB, Hendrickson WA
TitleStructure of beta 2-bungarotoxin: potassium channel binding by Kunitz modules and targeted phospholipase action.
Related PDB1bun
[10]
PubMed ID8829622
JournalBiochem Mol Biol Int
Year1996
Volume38
Pages617-23
AuthorsChang LS, Wen EY, Chang CC
TitleThe structural elements of phospholipase A2 affecting the enhancement of 8-anilinonaphthalene-1-sulfonate fluorescence.
[11]
PubMed ID9161720
JournalBiochem Mol Biol Int
Year1997
Volume41
Pages1247-53
AuthorsChang LS, Chang CC, Wu PF
TitleThe structural and functional essentiality of the N-terminal alpha-helix in the phospholipase A2 of the Taiwan banded krait.
[12]
PubMed ID11286555
JournalJ Mol Biol
Year2001
Volume307
Pages1049-59
AuthorsSingh G, Gourinath S, Sharma S, Paramasivam M, Srinivasan A, Singh TP
TitleSequence and crystal structure determination of a basic phospholipase A2 from common krait (Bungarus caeruleus) at 2.4 A resolution: identification and characterization of its pharmacological sites.
[13]
CommentsREVIEW.
Medline ID20396379
PubMed ID10936627
JournalToxicon
Year2001
Volume39
Pages107-18
AuthorsRowan EG
TitleWhat does beta-bungarotoxin do at the neuromuscular junction?
Related UniProtKBP00617,P00989

comments
This protein, beta-bungarotoxin, is one of snake venom toxin. It is composed of a phospholipase A2 subunit (A chain) and a smaller Kunitz-type protease inhibitor-like subunit (B chain), which are coupled covalently through a disulfide bond (see [9]).

createdupdated
2004-11-192009-02-26


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