Sequence of BLAC_STAAU
EC Number:3.5.2.6
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
a beta-lactam + H2O = a substituted beta-amino acid
Other sequences found for EC No. 3.5.2.6
General information:
Sequence
0 MKKLIFLIVI ALVLSACNSN SSHAKELNDL EKKYNAHIGV YALDTKSGKE VKFNSDKRFA
60 YASTSKAINS AILLEQVPYN KLNKKVHINK DDIVAYSPIL EKYVGKDITL KALIEASMTY
120 SDNTANNKII KEIGGIKKVK QRLKELGDKV TNPVRYEIEL NYYSPKSKKD TSTPAAFGKT
180 LNKLIANGKL SKENKKFLLD LMLNNKSGDT LIKDGVPKDY KVADKSGQAI TYASRNDVAF
240 VYPKGQSEPI VLVIFTNKDN KSDKPNDKLI SETAKSVMKE F
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
774783
Chan P.T.
Nucleotide sequence of the Staphylococcus aureus PC1 beta-lactamase gene.
Nucleic Acids Res.
14
5940-5940
1986
774784
Gillspie M.T.,Skurray R.A.
Nucleotide sequence of the blaZ gene of the Staphylococcus aureus beta-lactamase transposon Tn4002.
Nucleic Acids Res.
17
8854-8854
1989
774785
Rowland S.J.,Dyke K.G.H.
Tn552, a novel transposable element from Staphylococcus aureus.
Mol. Microbiol.
4
961-975
1990
774786
Wang P.-Z.,Novick R.P.
Nucleotide sequence and expression of the beta-lactamase gene from Staphylococcus aureus plasmid pI258 in Escherichia coli, Bacillus subtilis, and Staphylococcus aureus.
J. Bacteriol.
169
1763-1766
1987
774787
McLaughlin J.R.,Murray C.L.,Rabinowitz J.C.
Unique features in the ribosome binding site sequence of the Gram-positive Staphylococcus aureus beta-lactamase gene.
J. Biol. Chem.
256
11283-11291
1981
774788
Ambler R.P.
The amino acid sequence of Staphylococcus aureus penicillinase.
Biochem. J.
151
197-218
1975
774789
Herzberg O.,Moult J.
Bacterial resistance to beta-lactam antibiotics: crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.5-A resolution.
Science
236
694-701
1987
774790
Herzberg O.
Refined crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.0-A resolution.
J. Mol. Biol.
217
701-719
1991
774791
Banerjee S.,Pieper U.,Kapadia G.,Pannell L.K.,Herzberg O.
Role of the omega-loop in the activity, substrate specificity, and structure of class A beta-lactamase.
Biochemistry
37
3286-3296
1998
774792
Chen C.C.,Herzberg O.
Relocation of the catalytic carboxylate group in class A beta-lactamase: the structure and function of the mutant enzyme Glu166-->Gln:Asn170-->Asp.
Protein Eng.
12
573-579
1999
