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Identification
HMDB Protein ID HMDBP00697
Secondary Accession Numbers
  • 5970
Name Argininosuccinate lyase
Synonyms
  1. ASAL
  2. Arginosuccinase
Gene Name ASL
Protein Type Enzyme
Biological Properties
General Function Involved in argininosuccinate lyase activity
Specific Function Not Available
Pathways
  • Alanine, aspartate and glutamate metabolism
  • Arginine and Proline Metabolism
  • Arginine and proline metabolism
  • Arginine: Glycine Amidinotransferase Deficiency (AGAT Deficiency)
  • Argininemia
  • Argininosuccinic Aciduria
  • Aspartate Metabolism
  • Canavan Disease
  • Carbamoyl Phosphate Synthetase Deficiency
  • Citrullinemia Type I
  • Creatine deficiency, guanidinoacetate methyltransferase deficiency
  • Guanidinoacetate Methyltransferase Deficiency (GAMT Deficiency)
  • Hyperornithinemia with gyrate atrophy (HOGA)
  • Hyperornithinemia-hyperammonemia-homocitrullinuria [HHH-syndrome]
  • Hyperprolinemia Type I
  • Hyperprolinemia Type II
  • Hypoacetylaspartia
  • L-arginine biosynthesis
  • L-arginine:glycine amidinotransferase deficiency
  • Ornithine Aminotransferase Deficiency (OAT Deficiency)
  • Ornithine Transcarbamylase Deficiency (OTC Deficiency)
  • Prolidase Deficiency (PD)
  • Prolinemia Type II
  • urea cycle
  • Urea Cycle
Reactions
Argininosuccinic acid → Fumaric acid + L-Arginine details
GO Classification
Biological Process
arginine catabolic process
urea cycle
arginine biosynthetic process via ornithine
internal protein amino acid acetylation
Cellular Component
cytosol
Function
catalytic activity
lyase activity
carbon-nitrogen lyase activity
amidine-lyase activity
argininosuccinate lyase activity
Molecular Function
argininosuccinate lyase activity
Process
arginine biosynthetic process
metabolic process
arginine metabolic process
cellular metabolic process
glutamine family amino acid metabolic process
arginine biosynthetic process via ornithine
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
Cellular Location Not Available
Gene Properties
Chromosome Location 7
Locus 7q11.21
SNPs ASL
Gene Sequence
>1395 bp
ATGGCCTCGGAGAGTGGGAAGCTTTGGGGTGGCCGGTTTGTGGGTGCAGTGGACCCCATC
ATGGAGAAGTTCAACGCGTCCATTGCCTACGACCGGCACCTTTGGGAGGTGGATGTTCAA
GGCAGCAAAGCCTACAGCAGGGGCCTGGAGAAGGCAGGGCTCCTCACCAAGGCCGAGATG
GACCAGATACTCCATGGCCTAGACAAGGTGGCTGAGGAGTGGGCCCAGGGCACCTTCAAA
CTGAACTCCAATGATGAGGACATCCACACAGCCAATGAGCGCCGCCTGAAGGAGCTCATT
GGTGCAACGGCAGGGAAGCTGCACACGGGACGGAGCCGGAATGACCAGGTGGTCACAGAC
CTCAGGCTGTGGATGCGGCAGACCTGCTCCACGCTCTCGGGCCTCCTCTGGGAGCTCATT
AGGACCATGGTGGATCGGGCAGAGGCGGAACGTGATGTTCTCTTCCCGGGGTACACCCAT
TTGCAGAGGGCCCAGCCCATCCGCTGGAGCCACTGGATTCTGAGCCACGCCGTGGCACTG
ACCCGAGACTCTGAGCGGCTGCTGGAGGTGCGGAAGCGGATCAATGTCCTGCCCCTGGGG
AGTGGGGCCATTGCAGGCAATCCCCTGGGTGTGGACCGAGAGCTGCTCCGAGCAGAACTC
AACTTTGGGGCCATCACTCTCAACAGCATGGATGCCACTAGTGAGCGGGACTTTGTGGCC
GAGTTCCTGTTCTGGCGTTCGCTGTGCATGACCCATCTCAGCAGGATGGCCGAGGACCTC
ATCCTCTACTGCACCAAGGAATTCAGCTTCGTGCAGCTCTCAGATGCCTACAGCACGGGA
AGCAGCCTGATGCCCCAGAAGAAAAACCCCGACAGTTTGGAGCTGATCCGGAGCAAGGCT
GGGCGTGTGTTTGGGCGGTGTGCCGGGCTCCTGATGACCCTCAAGGGACTTCCCAGCACC
TACAACAAAGACTTACAGGAGGACAAGGAAGCTGTGTTTGAAGTGTCAGACACTATGAGT
GCCGTGCTCCAGGTGGCCACTGGCGTCATCTCTACGCTGCAGATTCACCAAGAGAACATG
GGACAGGCTCTCAGCCCCGACATGCTGGCCACTGACCTTGCCTATTACCTGGTCCGCAAA
GGGATGCCATTCCGCCAGGCCCATGAGGCCTCCGGGAAAGCTGTGTTCATGGCCGAGACC
AAGGGGGTCGCCCTCAACCAGCTGTCACTGCAGGAGCTGCAGACCATCAGCCCCCTGTTC
TCGGGCGACGTGATCTGCGTGTGGGACTACCGGCACAGTGTGGAGCAGTATGGTGCCCTG
GGCGGCACTGCGCGCTCCAGCGTCGACTGGCAAATCCGCCAGGTGCGGGCGCTACTGCAG
GCACAGCAGGCCTAG
Protein Properties
Number of Residues 464
Molecular Weight 51657.505
Theoretical pI 6.48
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Argininosuccinate lyase
MASESGKLWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEM
DQILHGLDKVAEEWAQGTFKLNSNDEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTD
LRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVAL
TRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVA
EFLFWASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKA
GRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENM
GQALSPDMLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVALNQLSLQELQTISPLF
SGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQAQQA
GenBank ID Protein 28878
UniProtKB/Swiss-Prot ID P04424
UniProtKB/Swiss-Prot Entry Name ARLY_HUMAN
PDB IDs
GenBank Gene ID Y00753
GeneCard ID ASL
GenAtlas ID ASL
HGNC ID HGNC:746
References
General References
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  2. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed:16959974 ]
  3. Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL: Regulation of cellular metabolism by protein lysine acetylation. Science. 2010 Feb 19;327(5968):1000-4. doi: 10.1126/science.1179689. [PubMed:20167786 ]
  4. Matuo S, Tatsuno M, Kobayashi K, Saheki T, Miyata T, Iwanaga S, Amaya Y, Mori M: Isolation of cDNA clones of human argininosuccinate lyase and corrected amino acid sequence. FEBS Lett. 1988 Jul 18;234(2):395-9. [PubMed:3391281 ]
  5. O'Brien WE, McInnes R, Kalumuck K, Adcock M: Cloning and sequence analysis of cDNA for human argininosuccinate lyase. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7211-5. [PubMed:3463959 ]
  6. Todd S, McGill JR, McCombs JL, Moore CM, Weider I, Naylor SL: cDNA sequence, interspecies comparison, and gene mapping analysis of argininosuccinate lyase. Genomics. 1989 Jan;4(1):53-9. [PubMed:2644168 ]
  7. Piatigorsky J, O'Brien WE, Norman BL, Kalumuck K, Wistow GJ, Borras T, Nickerson JM, Wawrousek EF: Gene sharing by delta-crystallin and argininosuccinate lyase. Proc Natl Acad Sci U S A. 1988 May;85(10):3479-83. [PubMed:3368457 ]
  8. Turner MA, Simpson A, McInnes RR, Howell PL: Human argininosuccinate lyase: a structural basis for intragenic complementation. Proc Natl Acad Sci U S A. 1997 Aug 19;94(17):9063-8. [PubMed:9256435 ]
  9. Sampaleanu LM, Vallee F, Thompson GD, Howell PL: Three-dimensional structure of the argininosuccinate lyase frequently complementing allele Q286R. Biochemistry. 2001 Dec 25;40(51):15570-80. [PubMed:11747432 ]
  10. Barbosa P, Cialkowski M, O'Brien WE: Analysis of naturally occurring and site-directed mutations in the argininosuccinate lyase gene. J Biol Chem. 1991 Mar 15;266(8):5286-90. [PubMed:1705937 ]
  11. Walker DC, McCloskey DA, Simard LR, McInnes RR: Molecular analysis of human argininosuccinate lyase: mutant characterization and alternative splicing of the coding region. Proc Natl Acad Sci U S A. 1990 Dec;87(24):9625-9. [PubMed:2263616 ]
  12. Kleijer WJ, Garritsen VH, Linnebank M, Mooyer P, Huijmans JG, Mustonen A, Simola KO, Arslan-Kirchner M, Battini R, Briones P, Cardo E, Mandel H, Tschiedel E, Wanders RJ, Koch HG: Clinical, enzymatic, and molecular genetic characterization of a biochemical variant type of argininosuccinic aciduria: prenatal and postnatal diagnosis in five unrelated families. J Inherit Metab Dis. 2002 Sep;25(5):399-410. [PubMed:12408190 ]
  13. Trevisson E, Salviati L, Baldoin MC, Toldo I, Casarin A, Sacconi S, Cesaro L, Basso G, Burlina AB: Argininosuccinate lyase deficiency: mutational spectrum in Italian patients and identification of a novel ASL pseudogene. Hum Mutat. 2007 Jul;28(7):694-702. [PubMed:17326097 ]