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Sequence of ASPG_PYRFU

EC Number:3.5.1.1

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
asparaginase
Q8TZE8
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
326
35765
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 MKILLIGMGG TIASVKGENG YEASLSVKEV LDIAGIKDCE DCDFLDLKNV DSTLIQPEDW
 60 VDLAETLYKN VKKYDGIIVT HGTDTLAYTS SMISFMLRNP PIPIVFTGSM IPATEENSDA
120 PLNLQTAIKF ATSGIRGVYV AFNGKVMLGV RTSKVRTMSR DAFESINYPI IAELRGEDLV
180 VNFIPKFNNG EVTLDLRHDP KVLVIKLIPG LSGDIFRAAV ELGYRGIVIE GYGAGGIPYR
240 GSDLLQTIEE LSKEIPIVMT TQAMYDGVDL TRYKVGRLAL RAGVIPAGDM TKEATVTKLM
300 WILGHTNNVE EIKVLMRKNL VGELRD
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
900505
Maeder D.L.,Weiss R.B.,Dunn D.M.,Cherry J.L.,Gonzalez J.M.,DiRuggiero J.,Robb F.T.
Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.
Genetics
152
1299-1305
1999
900506
Bansal S.,Gnaneswari D.,Mishra P.,Kundu B.
Structural stability and functional analysis of L-asparaginase from Pyrococcus furiosus.
Biochemistry (Mosc.)
75
375-381
2010
900507
Bansal S.,Srivastava A.,Mukherjee G.,Pandey R.,Verma A.K.,Mishra P.,Kundu B.
Hyperthermophilic asparaginase mutants with enhanced substrate affinity and antineoplastic activity: structural insights on their mechanism of action.
FASEB J.
26
1161-1171
2012
900508
Tomar R.,Garg D.K.,Mishra R.,Thakur A.K.,Kundu B.
N-terminal domain of Pyrococcus furiosus L-asparaginase functions as a non-specific, stable, molecular chaperone.
FEBS J.
280
2688-2699
2013
900509
Garg D.K.,Tomar R.,Dhoke R.R.,Srivastava A.,Kundu B.
Domains of Pyrococcus furiosus L-asparaginase fold sequentially and assemble through strong intersubunit associative forces.
Extremophiles
19
681-691
2015
900510
Tomar R.,Sharma P.,Srivastava A.,Bansal S.,Ashish F.,Kundu B.
Structural and functional insights into an archaeal L-asparaginase obtained through the linker-less assembly of constituent domains.
Acta Crystallogr. D
70
3187-3197
2014