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Sequence of AHLLA_BACTK

EC Number:3.1.1

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
P0CJ63
Bacillus thuringiensis subsp. kurstaki
250
28220
Reaction
Other sequences found for EC No. 3.1.1

EC Number:3.1.1.25

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
1,4-lactonase
P0CJ63
Bacillus thuringiensis subsp. kurstaki
250
28220
Reaction
a 1,4-lactone + H2O = a 4-hydroxyacid
Other sequences found for EC No. 3.1.1.25

EC Number:3.1.1.81

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
quorum-quenching N-acyl-homoserine lactonase
P0CJ63
Bacillus thuringiensis subsp. kurstaki
250
28220
Reaction
an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
Other sequences found for EC No. 3.1.1.81

General information:

Sequence
show sequence in fasta format
  0 MTVKKLYFIP AGRCMLDHSS VNSALTPGKL LNLPVWCYLL ETEEGPILVD TGMPESAVNN
 60 EGLFNGTFVE GQILPKMTEE DRIVNILKRV GYEPDDLLYI ISSHLHFDHA GGNGAFTNTP
120 IIVQRTEYEA ALHREEYMKE CILPHLNYKI IEGDYEVVPG VQLLYTPGHS PGHQSLFIET
180 EQSGSVLLTI DASYTKENFE DEVPFAGFDP ELALSSIKRL KEVVKKEKPI IFFGHDIEQE
240 KSCRVFPEYI
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
512649
Dong Y.H.,Gusti A.R.,Zhang Q.,Xu J.L.,Zhang L.H.
Identification of quorum-quenching N-acyl homoserine lactonases from Bacillus species.
Appl. Environ. Microbiol.
68
1754-1759
2002
512650
Lee S.J.,Park S.Y.,Lee J.J.,Yum D.Y.,Koo B.T.,Lee J.K.
Genes encoding the N-acyl homoserine lactone-degrading enzyme are widespread in many subspecies of Bacillus thuringiensis.
Appl. Environ. Microbiol.
68
3919-3924
2002
512651
Momb J.,Wang C.,Liu D.,Thomas P.W.,Petsko G.A.,Guo H.,Ringe D.,Fast W.
Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 2. Substrate modeling and active site mutations.
Biochemistry
47
7715-7725
2008
512652
Liu D.,Lepore B.W.,Petsko G.A.,Thomas P.W.,Stone E.M.,Fast W.,Ringe D.
Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis.
Proc. Natl. Acad. Sci. U.S.A.
102
11882-11887
2005
512653
Kim M.H.,Choi W.C.,Kang H.O.,Lee J.S.,Kang B.S.,Kim K.J.,Derewenda Z.S.,Oh T.K.,Lee C.H.,Lee J.K.
The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase.
Proc. Natl. Acad. Sci. U.S.A.
102
17606-17611
2005
512654
Liu D.,Momb J.,Thomas P.W.,Moulin A.,Petsko G.A.,Fast W.,Ringe D.
Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures.
Biochemistry
47
7706-7714
2008