L-asparaginase 2
Details
- Name
- L-asparaginase 2
- Kind
- protein
- Synonyms
- 3.5.1.1
- L-ASNase II
- L-asparaginase II
- L-asparagine amidohydrolase II
- Gene Name
- ansB
- UniProtKB Entry
- P00805Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- 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
- Functionsasparaginase activity / identical protein bindingProcessesasparagine metabolic process / protein homotetramerizationComponentscytosol / outer membrane-bounded periplasmic space / periplasmic space
- General Function
- Not Available
- Specific Function
- asparaginase activity
- Pfam Domain Function
- Asparaginase (PF00710)
- Signal Regions
- 1-22
- 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
Resource Link UniProtKB ID P00805 UniProtKB Entry Name ASPG2_ECOLI GenBank Protein ID 146597 GenBank Gene ID M34277 PDB ID(s) 1HO3, 1IHD, 1JAZ, 1JJA, 1NNS, 3ECA, 4ECA KEGG ID ecj:JW2924 NCBI Gene ID 947454 - General References
- 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]
- 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]
- 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]
- 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]
- Maita T, Matsuda G: The primary structure of L-asparaginase from Escherichia coli. Hoppe Seylers Z Physiol Chem. 1980;361(2):105-17. [Article]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Threonine-Aspartic Ester experimental unknown target Details