Isoaspartyl peptidase/L-asparaginase

NameIsoaspartyl peptidase/L-asparaginase
Synonyms
  • 3.4.19.5
  • ALP
  • Asparaginase-like protein 1
  • Beta-aspartyl-peptidase
  • CRASH
  • Isoaspartyl dipeptidase
  • L-asparagine amidohydrolase
Gene NameASRGL1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0037176|Isoaspartyl peptidase/L-asparaginase
MNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPE
FNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQ
GAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTDCQKNLGTVGAVALDCKGNV
AYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQ
GKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPD
DTTITDLP
Number of residues308
Molecular Weight32054.325
Theoretical pI5.65
GO Classification
Functions
  • beta-aspartyl-peptidase activity
  • asparaginase activity
Processes
  • cellular nitrogen compound metabolic process
  • small molecule metabolic process
  • L-phenylalanine catabolic process
  • asparagine catabolic process via L-aspartate
Components
  • cytosol
  • cytoplasm
  • nucleus
General FunctionBeta-aspartyl-peptidase activity
Specific FunctionHas both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID127798426
UniProtKB IDQ7L266
UniProtKB Entry NameASGL1_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0019256|Isoaspartyl peptidase/L-asparaginase (ASRGL1)
ATGAATCCCATCGTAGTGGTCCACGGCGGCGGAGCCGGTCCCATCTCCAAGGATCGGAAG
GAGCGAGTGCACCAGGGCATGGTCAGAGCCGCCACCGTGGGCTACGGCATCCTCCGGGAG
GGCGGGAGCGCCGTGGATGCCGTAGAGGGAGCTGTCGTCGCCCTGGAAGACGATCCCGAG
TTCAACGCAGGTTGTGGGTCTGTCTTGAACACAAATGGTGAGGTTGAAATGGATGCTAGT
ATCATGGATGGAAAAGACCTGTCTGCAGGAGCAGTGTCCGCAGTCCAGTGTATAGCAAAT
CCCATTAAACTTGCTCGGCTTGTCATGGAAAAGACACCTCATTGCTTTCTGACTGACCAA
GGCGCAGCGCAGTTTGCAGCAGCTATGGGGGTTCCAGAGATTCCTGGAGAAAAACTGGTG
ACAGAGAGAAACAAAAAGCGCCTGGAAAAAGAGAAGCATGAAAAAGGTGCTCAGAAAACA
GATTGTCAAAAAAACTTGGGAACCGTGGGTGCTGTTGCCTTGGACTGCAAAGGGAATGTA
GCCTACGCAACCTCCACAGGCGGTATCGTTAATAAAATGGTCGGCCGCGTTGGGGACTCA
CCGTGTCTAGGAGCTGGAGGTTATGCCGACAATGACATCGGAGCCGTCTCAACCACAGGG
CATGGGGAAAGCATCCTGAAGGTGAACCTGGCTAGACTCACCCTGTTCCACATAGAACAA
GGAAAGACGGTAGAAGAGGCTGCGGACCTATCGTTGGGTTATATGAAGTCAAGGGTTAAA
GGTTTAGGTGGCCTCATCGTGGTTAGCAAAACAGGAGACTGGGTGGCAAAGTGGACCTCC
ACCTCCATGCCCTGGGCAGCCGCCAAGGACGGCAAGCTGCACTTCGGAATTGATCCTGAC
GATACTACTATCACCGACCTTCCCTAA
GenBank Gene IDBC021295
GeneCard IDNot Available
GenAtlas IDASRGL1
HGNC IDHGNC:16448
Chromosome Location11
Locus11q12.3
References
  1. Bush LA, Herr JC, Wolkowicz M, Sherman NE, Shore A, Flickinger CJ: A novel asparaginase-like protein is a sperm autoantigen in rats. Mol Reprod Dev. 2002 Jun;62(2):233-47. 11984834
  2. Evtimova V, Zeillinger R, Kaul S, Weidle UH: Identification of CRASH, a gene deregulated in gynecological tumors. Int J Oncol. 2004 Jan;24(1):33-41. 14654938
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  5. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. 19413330
  6. Cantor JR, Stone EM, Chantranupong L, Georgiou G: The human asparaginase-like protein 1 hASRGL1 is an Ntn hydrolase with beta-aspartyl peptidase activity. Biochemistry. 2009 Nov 24;48(46):11026-31. doi: 10.1021/bi901397h. 19839645
  7. Nomme J, Su Y, Konrad M, Lavie A: Structures of apo and product-bound human L-asparaginase: insights into the mechanism of autoproteolysis and substrate hydrolysis. Biochemistry. 2012 Aug 28;51(34):6816-26. Epub 2012 Aug 14. 22861376
  8. Li W, Cantor JR, Yogesha SD, Yang S, Chantranupong L, Liu JQ, Agnello G, Georgiou G, Stone EM, Zhang Y: Uncoupling intramolecular processing and substrate hydrolysis in the N-terminal nucleophile hydrolase hASRGL1 by circular permutation. ACS Chem Biol. 2012 Nov 16;7(11):1840-7. doi: 10.1021/cb300232n. Epub 2012 Aug 29. 22891768