L-asparaginase 2

Details

Name
L-asparaginase 2
Synonyms
  • 3.5.1.1
  • L-ASNase II
  • L-asparaginase II
  • L-asparagine amidohydrolase II
Gene Name
ansB
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0016398|L-asparaginase 2
MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNA
VPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYF
LDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGR
DVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVY
NYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGAT
TQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY
Number of residues
348
Molecular Weight
36850.455
Theoretical pI
6.29
GO Classification
Functions
asparaginase activity / identical protein binding
Processes
asparagine metabolic process / protein homotetramerization
Components
cytosol / outer membrane-bounded periplasmic space / periplasmic space
General Function
Identical protein binding
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0016399|L-asparaginase 2 (ansB)
ATGGAGTTTTTCAAAAAGACGGCACTTGCCGCACTGGTTATGGGTTTTAGTGGTGCAGCA
TTGGCATTACCCAATATCACCATTTTAGCAACCGGCGGGACCATTGCCGGTGGTGGTGAC
TCCGCAACCAAATCTAACTACACAGTGGGTAAAGTTGGCGTAGAAAATCTGGTTAATGCG
GTGCCGCAACTAAAAGACATTGCGAACGTTAAAGGCGAGCAGGTAGTGAATATCGGCTCC
CAGGACATGAACGATAATGTCTGGCTGACACTGGCGAAAAAAATTAACACCGACTGCGAT
AAGACCGACGGCTTCGTCATTACCCACGGTACCGACACGATGGAAGAAACTGCTTACTTC
CTCGACCTGACGGTGAAATGCGACAAACCGGTGGTGATGGTCGGCGCAATGCGTCCGTCC
ACGTCTATGAGCGCAGACGGTCCATTCAACCTGTATAACGCGGTAGTGACCGCAGCTGAT
AAAGCCTCCGCCAACCGTGGCGTGCTGGTAGTGATGAATGACACCGTGCTTGATGGCCGT
GACGTCACCAAAACCAACACCACCGACGTAGCGACCTTCAAGTCTGTTAACTACGGTCCT
CTGGGTTACATTCACAACGGTAAGATTGACTACCAGCGTACCCCGGCACGTAAGCATACC
AGCGACACGCCATTCGATGTCTCTAAGCTGAATGAACTGCCGAAAGTCGGCATTGTTTAT
AACTACGCTAACGCATCCGATCTTCCGGCTAAAGCACTGGTAGATGCGGGCTATGATGGC
ATCGTTAGCGCTGGTGTGGGTAACGGCAACCTGTATAAATCTGTGTTCGACACGCTGGCG
ACCGCCGCGAAAACCGGTACTGCAGTCGTGCGTTCTTCCCGCGTACCGACGGGCGCTACC
ACTCAGGATGCCGAAGTGGATGATGCGAAATACGGCTTCGTCGCCTCTGGCACGCTGAAC
CCGCAAAAAGCGCGCGTTCTGCTGCAACTGGCTCTGACGCAAACCAAAGATCCGCAGCAG
ATCCAGCAGATCTTCAATCAGTACTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00805
UniProtKB Entry NameASPG2_ECOLI
GenBank Protein ID146597
GenBank Gene IDM34277
General References
  1. Jennings MP, Beacham IR: Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB, and its regulation by cyclic AMP receptor and FNR proteins. J Bacteriol. 1990 Mar;172(3):1491-8. [Article]
  2. Bonthron DT: L-asparaginase II of Escherichia coli K-12: cloning, mapping and sequencing of the ansB gene. Gene. 1990 Jul 2;91(1):101-5. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Maita T, Matsuda G: The primary structure of L-asparaginase from Escherichia coli. Hoppe Seylers Z Physiol Chem. 1980;361(2):105-17. [Article]
  6. Maita T, Morokuma K, Matsuda G: Amino acid sequences of the tryptic peptides from carboxymethylated L-asparaginase from Escherichia coli. Hoppe Seylers Z Physiol Chem. 1979 Oct;360(10):1483-95. [Article]
  7. Peterson RG, Richards FF, Handschumacher RE: Structure of peptide from active site region of Escherichia coli L-asparaginase. J Biol Chem. 1977 Mar 25;252(6):2072-6. [Article]
  8. Greenquist AC, Wriston JC Jr: Chemical evidence for identical subunits in L-asparaginase from Escherichia coli B. Arch Biochem Biophys. 1972 Sep;152(1):280-6. [Article]
  9. Harms E, Wehner A, Aung HP, Rohm KH: A catalytic role for threonine-12 of E. coli asparaginase II as established by site-directed mutagenesis. FEBS Lett. 1991 Jul 8;285(1):55-8. [Article]
  10. Wehner A, Harms E, Jennings MP, Beacham IR, Derst C, Bast P, Rohm KH: Site-specific mutagenesis of Escherichia coli asparaginase II. None of the three histidine residues is required for catalysis. Eur J Biochem. 1992 Sep 1;208(2):475-80. [Article]
  11. Derst C, Henseling J, Rohm KH: Probing the role of threonine and serine residues of E. coli asparaginase II by site-specific mutagenesis. Protein Eng. 1992 Dec;5(8):785-9. [Article]
  12. Swain AL, Jaskolski M, Housset D, Rao JK, Wlodawer A: Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy. Proc Natl Acad Sci U S A. 1993 Feb 15;90(4):1474-8. [Article]
  13. Palm GJ, Lubkowski J, Derst C, Schleper S, Rohm KH, Wlodawer A: A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant. FEBS Lett. 1996 Jul 22;390(2):211-6. [Article]
  14. Sanches M, Barbosa JA, de Oliveira RT, Abrahao Neto J, Polikarpov I: Structural comparison of Escherichia coli L-asparaginase in two monoclinic space groups. Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):416-22. Epub 2003 Feb 21. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01817Threonine-Aspartic EsterexperimentalunknownDetails