Canmetcon
Identification
Name:L-asparaginase 2
Synonyms:
  • L-asparaginase II
  • L-ASNase II
  • L-asparagine amidohydrolase II
  • Colaspase
Gene Name:ansB
Enzyme Class:
Biological Properties
General Function:Involved in asparaginase activity
Specific Function:L-asparagine + H(2)O = L-aspartate + NH(3)
Cellular Location:Periplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb
SMPDB Reactions:
L-Asparagine+Thumb+ThumbL-Aspartic acid+Thumb+Thumb
L-Asparagine + Water + L-Asparagine → L-Aspartic acid + Ammonium + L-Aspartic acid
ReactionCard
EcoCyc Reactions:
Thumb+ThumbThumb+Thumb+Thumb
Complex Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB00051AmmoniaMetaboCard
ECMDB21186AmmoniumMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00168L-AsparagineMetaboCard
ECMDB00191L-Aspartic acidMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB00641L-GlutamineMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
asparaginase activity
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Process
asparagine metabolic process
aspartate family amino acid metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process
Gene Properties
Blattner:b2957
Gene OrientationCounterclockwise
Centisome Percentage:66.77
Left Sequence End3097704
Right Sequence End3098750
Gene Sequence:
>1047 bp
ATGAACAGAACTGACGAACTCCGTACTGCGCGTATTGAGAGCCTGGTAACGCCCGCCGAA
CTCGCGCTACGGTATCCCGTAACGCCTGGCGTCGCCACCCATGTCACCGACTCCCGCCGC
AGAATTGAAAAAATACTGAATGGTGAAGATAAGCGACTGTTGGTCATTATTGGCCCCTGC
TCGATCCACGATCTCACCGCTGCAATGGAGTACGCCACCCGTCTGCAGTCGCTGCGCAAC
CAGTACCAGTCACGGCTGGAAATCGTAATGCGCACCTATTTTGAAAAACCACGAACTGTT
GTCGGCTGGAAAGGACTAATCTCCGATCCAGATTTAAACGGCAGCTATCGGGTAAATCAC
GGTCTGGAGCTGGCGCGCAAATTACTTTTACAGGTAAATGAGCTGGGCGTCCCAACCGCG
ACCGAGTTCCTCGATATGGTGACCGGTCAGTTTATTGCTGATTTAATCAGTTGGGGCGCG
ATTGGCGCACGTACTACCGAAAGTCAGATCCACCGCGAAATGGCTTCGGCACTCTCCTGT
CCGGTAGGTTTTAAAAATGGTACCGATGGCAATACGCGGATTGCTGTGGATGCTATCCGC
GCAGCCCGCGCCAGCCATATGTTCCTCTCGCCAGACAAAAATGGTCAGATGACCATCTAT
CAGACCAGCGGCAACCCGTATGGCCACATTATTATGCGTGGCGGCAAAAAACCGAATTAT
CATGCCGATGATATCGCCGCAGCCTGCGATACGCTGCACGAGTTTGATTTACCTGAACAT
CTGGTGGTGGATTTCAGCCACGGTAACTGCCAGAAGCAGCACCGTCGCCAGTTAGAAGTT
TGTGAGGATATTTGTCAGCAAATCCGCAATGGCTCTACGGCGATTGCTGGAATTATGGCG
GAAAGTTTCCTGCGCGAAGGAACGCAAAAAATCGTCGGCAGTCAGCCGCTCACTTACGGT
CAATCCATTACCGACCCGTGTCTGGGCTGGGAGGATACCGAACGCCTGGTCGAAAAACTC
GCCTCTGCGGTAGATACCCGCTTCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:348
Protein Molecular Weight:36851
Protein Theoretical pI:6
PDB File:1NNS
Signaling Regions:
  • 1-22
Transmembrane Regions:
  • None
Protein Sequence:
>L-asparaginase 2
MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNA
VPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYF
LDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGR
DVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVY
NYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGAT
TQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY
References
External Links:
ResourceLink
Uniprot ID:P00805
Uniprot Name:ASPG2_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742785
PDB ID:1NNS
Ecogene ID:EG10046
Ecocyc:EG10046
ColiBase:b2957
Kegg Gene:b2957
EchoBASE ID:EB0044
CCDB:ASPG2_ECOLI
BacMap:16130858
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Bonthron, D. T. (1990). "L-asparaginase II of Escherichia coli K-12: cloning, mapping and sequencing of the ansB gene." Gene 91:101-105. Pubmed: 2144836
  • Derst, C., Henseling, J., Rohm, K. H. (1992). "Probing the role of threonine and serine residues of E. coli asparaginase II by site-specific mutagenesis." Protein Eng 5:785-789. Pubmed: 1287659
  • Greenquist, A. C., Wriston, J. C. Jr (1972). "Chemical evidence for identical subunits in L-asparaginase from Escherichia coli B." Arch Biochem Biophys 152:280-286. Pubmed: 4561256
  • Harms, E., Wehner, A., Aung, H. P., Rohm, K. H. (1991). "A catalytic role for threonine-12 of E. coli asparaginase II as established by site-directed mutagenesis." FEBS Lett 285:55-58. Pubmed: 1906013
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Jennings, M. P., Beacham, I. R. (1990). "Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB, and its regulation by cyclic AMP receptor and FNR proteins." J Bacteriol 172:1491-1498. Pubmed: 2407723
  • Maita, T., Matsuda, G. (1980). "The primary structure of L-asparaginase from Escherichia coli." Hoppe Seylers Z Physiol Chem 361:105-117. Pubmed: 6766894
  • Maita, T., Morokuma, K., Matsuda, G. (1979). "Amino acid sequences of the tryptic peptides from carboxymethylated L-asparaginase from Escherichia coli." Hoppe Seylers Z Physiol Chem 360:1483-1495. Pubmed: 387570
  • Palm, G. J., Lubkowski, J., Derst, C., Schleper, S., Rohm, K. H., Wlodawer, A. (1996). "A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant." FEBS Lett 390:211-216. Pubmed: 8706862
  • Peterson, R. G., Richards, F. F., Handschumacher, R. E. (1977). "Structure of peptide from active site region of Escherichia coli L-asparaginase." J Biol Chem 252:2072-2076. Pubmed: 321449
  • Swain, A. L., Jaskolski, M., Housset, D., Rao, J. K., Wlodawer, A. (1993). "Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy." Proc Natl Acad Sci U S A 90:1474-1478. Pubmed: 8434007
  • Wehner, A., Harms, E., Jennings, M. P., Beacham, I. R., Derst, C., Bast, P., Rohm, K. H. (1992). "Site-specific mutagenesis of Escherichia coli asparaginase II. None of the three histidine residues is required for catalysis." Eur J Biochem 208:475-480. Pubmed: 1521538