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Sequence of IAAA_ECOLI

EC Number:3.4.19.5

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
beta-aspartyl-peptidase
P37595
Escherichia coli (strain K12)
321
33394
Reaction
Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide
Other sequences found for EC No. 3.4.19.5

EC Number:3.5.1.1

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
asparaginase
P37595
Escherichia coli (strain K12)
321
33394
Reaction
L-asparagine + H2O = L-aspartate + NH3
Other sequences found for EC No. 3.5.1.1

General information:

Sequence
show sequence in fasta format
  0 MGKAVIAIHG GAGAISRAQM SLQQELRYIE ALSAIVETGQ KMLEAGESAL DVVTEAVRLL
 60 EECPLFNAGI GAVFTRDETH ELDACVMDGN TLKAGAVAGV SHLRNPVLAA RLVMEQSPHV
120 MMIGEGAENF AFARGMERVS PEIFSTSLRY EQLLAARKEG ATVLDHSGAP LDEKQKMGTV
180 GAVALDLDGN LAAATSTGGM TNKLPGRVGD SPLVGAGCYA NNASVAVSCT GTGEVFIRAL
240 AAYDIAALMD YGGLSLAEAC ERVVMEKLPA LGGSGGLIAI DHEGNVALPF NTEGMYRAWG
300 YAGDTPTTGI YREKGDTVAT Q
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1071145
Oshima T.,Aiba H.,Baba T.,Fujita K.,Hayashi K.,Honjo A.,Ikemoto K.,Inada T.,Itoh T.,Kajihara M.,Kanai K.,Kashimoto K.,Kimura S.,Kitagawa M.,Makino K.,Masuda S.,Miki T.,Mizobuchi K.,Mori H.,Motomura K.,Nakamura Y.,Nashimoto H.,Nishio Y.,Saito N.,Sampei G.,Seki Y.,Tagami H.,Takemoto K.,Wada C.,Yamamoto Y.,Yano M.,Horiuchi T.
A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.
DNA Res.
3
137-155
1996
1071146
Blattner F.R.,Plunkett G. III,Bloch C.A.,Perna N.T.,Burland V.,Riley M.,Collado-Vides J.,Glasner J.D.,Rode C.K.,Mayhew G.F.,Gregor J.,Davis N.W.,Kirkpatrick H.A.,Goeden M.A.,Rose D.J.,Mau B.,Shao Y.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
1071147
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
1071148
Nohno T.,Kasai Y.,Saito T.
Cloning and sequencing of the Escherichia coli chlEN operon involved in molybdopterin biosynthesis.
J. Bacteriol.
170
4097-4102
1988
1071149
Hejazi M.,Piotukh K.,Mattow J.,Deutzmann R.,Volkmer-Engert R.,Lockau W.
Isoaspartyl dipeptidase activity of plant-type asparaginases.
Biochem. J.
364
129-136
2002
1071150
Borodovsky M.,Rudd K.E.,Koonin E.V.
Intrinsic and extrinsic approaches for detecting genes in a bacterial genome.
Nucleic Acids Res.
22
4756-4767
1994
1071151
Borek D.,Jaskolski M.
Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome.
Acta Crystallogr. D
56
1505-1507
2000
1071152
Parry J.,Clark D.P.
Identification of a CysB-regulated gene involved in glutathione transport in Escherichia coli.
FEMS Microbiol. Lett.
209
81-85
2002
1071153
Borek D.,Michalska K.,Brzezinski K.,Kisiel A.,Podkowinski J.,Bonthron D.T.,Krowarsch D.,Otlewski J.,Jaskolski M.
Expression, purification and catalytic activity of Lupinus luteus asparagine beta-amidohydrolase and its Escherichia coli homolog.
Eur. J. Biochem.
271
3215-3226
2004
1071155
Prahl A.,Pazgier M.,Hejazi M.,Lockau W.,Lubkowski J.
Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli.
Acta Crystallogr. D
60
1173-1176
2004
1071156
Michalska K.,Brzezinski K.,Jaskolski M.
Crystal structure of isoaspartyl aminopeptidase in complex with L-aspartate.
J. Biol. Chem.
280
28484-28491
2005
1071157
Michalska K.,Borek D.,Hernandez-Santoyo A.,Jaskolski M.
Crystal packing of plant-type L-asparaginase from Escherichia coli.
Acta Crystallogr. D
64
309-320
2008