L-asparaginase
Details
- Name
- L-asparaginase
- Synonyms
- 3.5.1.1
- asn
- L-ASNase
- L-asparagine amidohydrolase
- Gene Name
- ansB
- Organism
- Pectobacterium chrysanthemi
- Amino acid sequence
>lcl|BSEQ0016466|L-asparaginase MERWFKSLFVLVLFFVFTASAADKLPNIVILATGGTIAGSAATGTQTTGYKAGALGVDTL INAVPEVKKLANVKGEQFSNMASENMTGDVVLKLSQRVNELLARDDVDGVVITHGTDTVE ESAYFLHLTVKSDKPVVFVAAMRPATAISADGPMNLLEAVRVAGDKQSRGRGVMVVLNDR IGSARYITKTNASTLDTFKANEEGYLGVIIGNRIYYQNRIDKLHTTRSVFDVRGLTSLPK VDILYGYQDDPEYLYDAAIQHGVKGIVYAGMGAGSVSVRGIAGMRKAMEKGVVVIRSTRT GNGIVPPDEELPGLVSDSLNPAHARILLMLALTRTSDPKVIQEYFHTY
- Number of residues
- 348
- Molecular Weight
- 37574.855
- Theoretical pI
- 8.62
- GO Classification
- Functionsasparaginase activityProcessesasparagine metabolic process
- General Function
- Asparaginase activity
- Specific Function
- Not Available
- Pfam Domain Function
- Asparaginase (PF00710)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0003041|1047 bp ATGGAAAGATGGTTTAAATCTCTGTTTGTTCTGGTTTTATTTTTTGTTTTTACGGCGAGT GCGGCAGATAAACTGCCCAATATCGTTATCCTGGCGACCGGCGGTACAATTGCCGGCTCA GCGGCAACGGGTACCCAAACCACAGGTTACAAGGCTGGCGCGCTTGGCGTGGATACGCTA ATCAACGCTGTGCCTGAGGTGAAGAAACTGGCTAATGTGAAGGGGGAGCAGTTCTCCAAC ATGGCCAGCGAAAACATGACCGGTGATGTGGTGCTCAAGCTGAGCCAGCGTGTGAATGAA CTGCTGGCACGGGATGATGTGGATGGTGTGGTGATCACCCACGGGACCGACACGGTGGAA GAGTCGGCTTACTTTCTTCATCTGACGGTAAAAAGTGACAAGCCAGTGGTGTTTGTCGCA GCGATGCGTCCGGCAACGGCCATCAGTGCTGACGGCCCGATGAACCTGCTGGAAGCGGTA CGCGTGGCGGGTGACAAACAGTCTCGCGGTCGCGGCGTGATGGTGGTGCTTAATGATCGT ATCGGCTCTGCCCGCTACATCACCAAGACCAACGCCTCTACGCTGGATACGTTCAAGGCG AATGAAGAAGGCTACCTGGGCGTCATTATTGGTAACCGCATTTACTACCAAAACCGAATC GACAAGCTGCATACCACCCGGTCTGTGTTCGACGTGCGTGGCCTGACTTCGCTGCCGAAA GTCGACATTCTTTATGGCTATCAGGATGACCCGGAATATCTGTATGACGCGGCTATCCAG CATGGCGTAAAAGGTATCGTCTATGCCGGTATGGGCGCAGGTTCAGTGTCCGTTCGCGGT ATTGCCGGTATGCGCAAGGCGATGGAGAAAGGCGTTGTTGTGATCCGTTCTACCCGCACA GGCAATGGTATTGTGCCGCCGGATGAAGAGCTGCCAGGTCTGGTTTCTGACTCTCTTAAC CCGGCACATGCCCGCATTCTGTTGATGCTGGCATTGACTCGCACCAGTGATCCGAAAGTC ATTCAAGAGTATTTCCATACTTATTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P06608 UniProtKB Entry Name ASPG_DICCH GenBank Protein ID 4185897 GenBank Gene ID X14777 - General References
- Minton NP, Bullman HM, Scawen MD, Atkinson T, Gilbert HJ: Nucleotide sequence of the Erwinia chrysanthemi NCPPB 1066 L-asparaginase gene. Gene. 1986;46(1):25-35. [Article]
- Filpula D, Nagle JW, Pulford S, Anderson DM: Sequence of L-asparaginase gene from Erwinia chrysanthemi NCPPB 1125. Nucleic Acids Res. 1988 Nov 11;16(21):10385. [Article]
- Tanaka S, Robinson EA, Appella E, Miller M, Ammon HL, Roberts J, Weber IT, Wlodawer A: Structures of amidohydrolases. Amino acid sequence of a glutaminase-asparaginase from Acinetobacter glutaminasificans and preliminary crystallographic data for an asparaginase from Erwinia chrysanthemi. J Biol Chem. 1988 Jun 25;263(18):8583-91. [Article]
- Miller M, Rao JK, Wlodawer A, Gribskov MR: A left-handed crossover involved in amidohydrolase catalysis. Crystal structure of Erwinia chrysanthemi L-asparaginase with bound L-aspartate. FEBS Lett. 1993 Aug 16;328(3):275-9. [Article]
- Aghaiypour K, Wlodawer A, Lubkowski J: Structural basis for the activity and substrate specificity of Erwinia chrysanthemi L-asparaginase. Biochemistry. 2001 May 15;40(19):5655-64. [Article]
- Aghaiypour K, Wlodawer A, Lubkowski J: Do bacterial L-asparaginases utilize a catalytic triad Thr-Tyr-Glu? Biochim Biophys Acta. 2001 Dec 17;1550(2):117-28. [Article]
- Lubkowski J, Dauter M, Aghaiypour K, Wlodawer A, Dauter Z: Atomic resolution structure of Erwinia chrysanthemi L-asparaginase. Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):84-92. Epub 2002 Dec 19. [Article]