L-asparaginase 2 (P00805)

• L-asparaginase II
• L-ASNase II
• L-asparagine amidohydrolase II
• Colaspase

• 3.5.1.1

• Asparagine biosynthesis PW000813
• Nitrogen metabolism PW000755

• Alanine, aspartate and glutamate metabolism ec00250
• Cyanoamino acid metabolism ec00460
• Metabolic pathways eco01100
• Nitrogen metabolism ec00910

>1047 bp
ATGAACAGAACTGACGAACTCCGTACTGCGCGTATTGAGAGCCTGGTAACGCCCGCCGAA
CTCGCGCTACGGTATCCCGTAACGCCTGGCGTCGCCACCCATGTCACCGACTCCCGCCGC
AGAATTGAAAAAATACTGAATGGTGAAGATAAGCGACTGTTGGTCATTATTGGCCCCTGC
TCGATCCACGATCTCACCGCTGCAATGGAGTACGCCACCCGTCTGCAGTCGCTGCGCAAC
CAGTACCAGTCACGGCTGGAAATCGTAATGCGCACCTATTTTGAAAAACCACGAACTGTT
GTCGGCTGGAAAGGACTAATCTCCGATCCAGATTTAAACGGCAGCTATCGGGTAAATCAC
GGTCTGGAGCTGGCGCGCAAATTACTTTTACAGGTAAATGAGCTGGGCGTCCCAACCGCG
ACCGAGTTCCTCGATATGGTGACCGGTCAGTTTATTGCTGATTTAATCAGTTGGGGCGCG
ATTGGCGCACGTACTACCGAAAGTCAGATCCACCGCGAAATGGCTTCGGCACTCTCCTGT
CCGGTAGGTTTTAAAAATGGTACCGATGGCAATACGCGGATTGCTGTGGATGCTATCCGC
GCAGCCCGCGCCAGCCATATGTTCCTCTCGCCAGACAAAAATGGTCAGATGACCATCTAT
CAGACCAGCGGCAACCCGTATGGCCACATTATTATGCGTGGCGGCAAAAAACCGAATTAT
CATGCCGATGATATCGCCGCAGCCTGCGATACGCTGCACGAGTTTGATTTACCTGAACAT
CTGGTGGTGGATTTCAGCCACGGTAACTGCCAGAAGCAGCACCGTCGCCAGTTAGAAGTT
TGTGAGGATATTTGTCAGCAAATCCGCAATGGCTCTACGGCGATTGCTGGAATTATGGCG
GAAAGTTTCCTGCGCGAAGGAACGCAAAAAATCGTCGGCAGTCAGCCGCTCACTTACGGT
CAATCCATTACCGACCCGTGTCTGGGCTGGGAGGATACCGAACGCCTGGTCGAAAAACTC
GCCTCTGCGGTAGATACCCGCTTCTGA

• Asparaginase (PF00710 )

• 1-22

• None

>L-asparaginase 2
MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNA
VPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYF
LDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGR
DVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVY
NYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGAT
TQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY

• 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