Crystal structure of duck argininosuccinate lyase with bound argininosuccinate.[1]
Identifiers
EC no.
4.3.2.1
CAS no.
9027-34-3
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BRENDA entry
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proteins
Argininosuccinate lyase
Crystallographic structure of the human ASL monomer with labeled domains.[2]
Identifiers
Symbol
ASL
NCBI gene
435
HGNC
746
OMIM
608310
RefSeq
NM_000048
UniProt
P04424
Other data
EC number
4.3.2.1
Locus
Chr. 7 pter-q22
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Structures
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The enzyme argininosuccinate lyase (EC 4.3.2.1, ASL, argininosuccinase; systematic name 2-(N ω-L-arginino)succinate arginine-lyase (fumarate-forming)) catalyzes the reversible breakdown of argininosuccinate:
Located in liver cytosol, it is the fourth enzyme of the urea cycle and involved in the biosynthesis of arginine in all species and the production of urea in ureotelic species.[2] Mutations resulting in low activity of the enzyme increase levels of urea in the body and result in various side effects.
The ASL gene is located on chromosome 7 between the centromere (junction of the long and short arm) and the long (q) arm at position 11.2, from base pair 64,984,963 to base pair 65,002,090.
ASL is related to intragenic complementation.[3][4][5]
^PDB: 1TJW; Sampaleanu LM, Codding PW, Lobsanov YD, Tsai M, Smith GD, Horvatin C, Howell PL (December 2004). "Structural studies of duck delta2 crystallin mutants provide insight into the role of Thr161 and the 280s loop in catalysis". Biochem. J. 384 (Pt 2): 437–47. doi:10.1042/BJ20040656. PMC 1134128. PMID 15320872.
^Turner MA, Simpson A, McInnes RR, Howell PL (August 1997). "Human argininosuccinate lyase: a structural basis for intragenic complementation". Proc. Natl. Acad. Sci. U.S.A. 94 (17): 9063–8. Bibcode:1997PNAS...94.9063T. doi:10.1073/pnas.94.17.9063. PMC 23030. PMID 9256435.
^Yu B, Howell PL (October 2000). "Intragenic complementation and the structure and function of argininosuccinate lyase". Cell. Mol. Life Sci. 57 (11): 1637–51. doi:10.1007/PL00000646. PMC 11147086. PMID 11092456. S2CID 1254964.
^Yu B, Thompson GD, Yip P, Howell PL, Davidson AR (December 2001). "Mechanisms for intragenic complementation at the human argininosuccinate lyase locus". Biochemistry. 40 (51): 15581–90. doi:10.1021/bi011526e. PMID 11747433.
and 16 Related for: Argininosuccinate lyase information
kidneys.[citation needed] In argininosuccinic aciduria, the enzyme argininosuccinatelyase, involved in the conversion of arginino succinate to arginine within...
synthetase I OTC Ornithine transcarbamoylase ASS argininosuccinate synthetase ASL argininosuccinatelyase ARG1 arginase 1 Before the urea cycle begins ammonia...
phenomenon is referred to as intragenic complementation. In humans, argininosuccinatelyase (ASL) is a homotetrameric enzyme that can undergo intragenic complementation...
nitric oxide from arginine in endothelial cells. Argininosuccinate synthetase and argininosuccinatelyase recycle citrulline, a byproduct of nitric oxide...
enzymes argininosuccinate synthetase and argininosuccinatelyase. This is an energetically costly process, because for each molecule of argininosuccinate that...
reaction is argininosuccinate synthetase. Argininosuccinic acid is a precursor to fumarate in the citric acid cycle via argininosuccinatelyase. Argininosuccinate...
Wawrousek EF (May 1988). "Gene sharing by delta-crystallin and argininosuccinatelyase". Proceedings of the National Academy of Sciences of the United...
Arginosuccinase, EC 4.3.2.1 (argininosuccinatelyase), which catalyzes the formation of arginine and fumarate from argininosuccinate, the last step in the biosynthesis...
citrulline and aspartate using the enzymes argininosuccinate synthase 1 (ASS1) and argininosuccinatelyase (ASL). Consequently, depleting arginine can...
those from birds and reptiles related to lactate dehydrogenase and argininosuccinatelyase, those of mammals to alcohol dehydrogenase and quinone reductase...
synthetase deficiency, is a rare disease caused by a deficiency in argininosuccinate synthetase, an enzyme involved in excreting excess nitrogen from the...
(OAT), and this yields ornithine. Then, the enzymes citrulline and argininosuccinate convert ornithine to arginine. There are two distinct lysine biosynthetic...
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