Identification |
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Name | L-asparaginase 1 |
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Synonyms | - L-asparaginase I
- L-asparagine amidohydrolase I
- ASP I
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Gene Name | ASP1 |
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Enzyme Class | |
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Biological Properties |
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General Function | Involved in asparaginase activity |
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Specific Function | L-asparagine + H(2)O = L-aspartate + NH(3) |
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Cellular Location | Cytoplasm |
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SMPDB Pathways | |
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KEGG Pathways | Alanine, aspartate and glutamate metabolism | ec00250 | | Cyanoamino acid metabolism | ec00460 | | Nitrogen metabolism | ec00910 | |
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SMPDB Reactions | |
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KEGG Reactions | |
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Metabolites | YMDB ID | Name | View |
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YMDB00091 | Ammonia | Show | YMDB00226 | L-Asparagine | Show | YMDB00423 | Ammonium | Show | YMDB00890 | water | Show | YMDB00896 | L-Aspartic acid | Show |
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GO Classification | Component |
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Not Available | Function |
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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 | asparaginase activity | Process |
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metabolic process | cellular metabolic process | cellular amino acid and derivative metabolic process | cellular amino acid metabolic process | aspartate family amino acid metabolic process | asparagine metabolic process |
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Gene Properties |
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Chromosome Location | chromosome 4 |
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Locus | YDR321W |
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Gene Sequence | >1146 bp
ATGAAAAGCGATTCAGTTGAAATCACTACCATCTGCCCAGATGTTGAAAATTCTCAGTTT
GTTGTGCAAAGCAACTGTCCAGAGACTATTCCAGAGATTCTAAAGTCTCAAAATGCCGCT
GTGAATGGCAGCGGCATCGCTTGCCAACAACGTAGCTTACCAAGAATCAAAATCTTGGGT
ACCGGTGGTACTATTGCATCGAAAGCTATAGACTCCTCTCAAACTGCCGGCTATCATGTT
GACCTGACCATCCAAGATCTATTGGATGCCATTCCAGATATATCCAAGGTCTGTGACATT
GAATATGAGCAACTATGCAACGTGGATTCTAAAGACATAAACGAGGATATTCTTTATAAA
ATTTATAAGGGCGTCTCAGAATCGTTGCAGGCTTTTGACGGTATAGTTATTACCCATGGG
ACTGATACGCTATCTGAAACTGCATTCTTTATTGAAAGTACTATTGATGCTGGCGACGTT
CCTATTGTTTTTGTTGGTTCGATGCGTCCTTCAACCAGCGTTTCTGCTGATGGCCCTATG
AACCTTTACCAAGCAATTTGCATTGCTTCAAATCCAAAATCTAGAGGAAGAGGTGTTCTT
GTTTCCTTGAATGACCAAATTTCCTCTGGTTACTACATTACTAAGACGAATGCAAATAGT
TTGGATTCTTTTAATGTTAGACAAGGCTATTTAGGAAATTTTGTCAACAATGAAATTCAC
TACTATTATCCTCCTGTGAAACCGCAAGGTTGCCACAAATTCAAACTGAGAGTGGACGGT
AAGCATTTTAAATTACCAGAGGTTTGCATTTTATATGCTCACCAAGCCTTTCCGCCAGCT
ATAGTCAACTTAGTGGCAGATAAGTATGATGGTATTGTTCTTGCTACCATGGGTGCTGGT
TCATTGCCGGAGGAGGTCAATGAAACCTGCATGAAATTGAGTTTGCCGATCGTATATTCC
AAGAGATCGATGGATGGTATGGTGCCTATTGCCAACGTACCAAAGAAAGGTTCAAAGGAG
GATAATCTCATCGCATCTGGTTATCTAAGCCCTGAAAAGAGCAGAATCTTGTTACAATTA
TGTTTGGCAGGTAACTACACGTTGGAAGAAATTAAACATGTTTTCACTGGCGTCTATGGT
GGGTGA |
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Protein Properties |
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Pfam Domain Function | |
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Protein Residues | 381 |
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Protein Molecular Weight | 41394.80078 |
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Protein Theoretical pI | 5.08 |
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Signalling Regions | |
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Transmembrane Regions | |
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Protein Sequence | >L-asparaginase 1
MKSDSVEITTICPDVENSQFVVQSNCPETIPEILKSQNAAVNGSGIACQQRSLPRIKILG
TGGTIASKAIDSSQTAGYHVDLTIQDLLDAIPDISKVCDIEYEQLCNVDSKDINEDILYK
IYKGVSESLQAFDGIVITHGTDTLSETAFFIESTIDAGDVPIVFVGSMRPSTSVSADGPM
NLYQAICIASNPKSRGRGVLVSLNDQISSGYYITKTNANSLDSFNVRQGYLGNFVNNEIH
YYYPPVKPQGCHKFKLRVDGKHFKLPEVCILYAHQAFPPAIVNLVADKYDGIVLATMGAG
SLPEEVNETCMKLSLPIVYSKRSMDGMVPIANVPKKGSKEDNLIASGYLSPEKSRILLQL
CLAGNYTLEEIKHVFTGVYGG |
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References |
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External Links | |
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General Reference | - Sinclair, K., Warner, J. P., Bonthron, D. T. (1994). "The ASP1 gene of Saccharomyces cerevisiae, encoding the intracellular isozyme of L-asparaginase." Gene 144:37-43.8026756
- Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, M., Buitrago, M. J., Coster, F., Delaveau, T., del Rey, F., Dujon, B., Eide, L. G., Garcia-Cantalejo, J. M., Goffeau, A., Gomez-Peris, A., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867
- Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956
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