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ASL (argininosuccinate lyase) is a human gene that makes the protein argininosuccinate lyase, one of the enzymes controlling a series of reactions called the urea cycle. The ASL enzyme starts the reaction in which the amino acid arginine, a building block of proteins, is produced from argininosuccinate. [[{{{diversity_link}}}|Diversity]] {{{diversity}}} Binomial name Homo sapiens Linnaeus, 1758 Trinomial name {{{trinomial}}} Type Species {{{type_species}}} Subspecies Homo sapiens idaltu (extinct) Homo sapiens sapiens [[Image:{{{range_map}}}|{{{range_map_width}}}|]] Synonyms {{{synonyms}}} Homo (genus). ...
This stylistic schematic diagram shows a gene in relation to the double helix structure of DNA and to a chromosome (right). ...
A representation of the 3D structure of myoglobin, showing coloured alpha helices. ...
Ribbon diagram of the catalytically perfect enzyme TIM. An enzyme is a protein that catalyzes, or speeds up, a chemical reaction. ...
The Urea Cycle is a cycle of biochemical reactions occurring in many animal organisms that produces urea from ammonia. ...
In chemistry, an amino acid is any molecule that contains both amino and carboxylic acid functional groups. ...
Arginine (Arg) is an α-amino acid. ...
The urea cycle is a sequence of reactions in the cells of the liver. It processes excess nitrogen, generated when protein is used by the body, to make a compound called urea that is excreted by the kidneys. Eliminating the excess nitrogen in this way prevents it from accumulating in the form of ammonia, which is toxic. The liver is one of the largest internal organs of the human body. ...
General Name, Symbol, Number nitrogen, N, 7 Chemical series nonmetals Group, Period, Block 15, 2, p Appearance colorless Atomic mass 14. ...
Urea is an organic compound of carbon, nitrogen, oxygen and hydrogen, with the formula CON2H4 or (NH2)2CO. Urea is also known as carbamide, especially in the recommended International Non-proprietary Names (rINN) in use in Europe. ...
Human kidneys viewed from behind with spine removed The kidneys are bean-shaped excretory organs in vertebrates. ...
Ammonia is a compound of nitrogen and hydrogen with the formula NH3. ...
For a list of biologically injurious substances, including toxins and other materials, as well as their effects, see poison. ...
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. Chromosome 7 is one of the 23 pairs of chromosomes in humans. ...
The centromere is a region of a eukaryotic chromosome where the kinetochore is assembled. ...
In molecular biology, two nucleotides on opposite complementary DNA or RNA strands that are connected via hydrogen bonds are called a base pair (often abbreviated bp). ...
Related conditions
Argininosuccinic aciduria: Several different mutations in the ASL gene have been identified. A mutated ASL gene may make an argininosuccinate lyase enzyme that is shorter than normal or the wrong shape. Argininosuccinic aciduria is an inherited disorder that causes ammonia to accumulate in the blood. ...
In biology, mutations are changes to the genetic material (usually DNA or RNA). ...
The shape of an enzyme affects its ability to bring other substances together to start a chemical reaction. If the argininosuccinate lyase enzyme is misshapen, it cannot fulfill its role in the urea cycle. Excess nitrogen is not converted to urea for excretion, and toxic ammonia accumulates in the body.
References - [[|Linnebank M, Tschiedel E, Haberle J, Linnebank A, Willenbring H, Kleijer WJ, Koch HG, ]], () ({{{Month}}} 2002). [ Argininosuccinate lyase (ASL) deficiency: mutation analysis in 27 patients and a completed structure of the human ASL gene]. Hum Genet 111 (4-5): 350-9. . PMID 12384776
- [[|Reid Sutton V, Pan Y, Davis EC, Craigen WJ, ]], () ({{{Month}}} 2003). [ A mouse model of argininosuccinic aciduria: biochemical characterization]. Mol Genet Metab 78 (1): 11-6. . PMID 12559843
- [[|Tanaka T, Nagao M, Mori T, Tsutsumi H, ]], () ({{{Month}}} 2002). [ A novel stop codon mutation (X465Y) in the argininosuccinate lyase gene in a patient with argininosuccinic aciduria]. Tohoku J Exp Med 198 (2): 119-24. . PMID 12512996
- [[|Turner MA, Simpson A, McInnes RR, Howell PL, ]], () ({{{Month}}} 1997). [ Human argininosuccinate lyase: a structural basis for intragenic complementation]. Proc Natl Acad Sci U S A 94 (17): 9063-8. . PMID 9256435
- [[|Yu B, Howell PL, ]], () ({{{Month}}} 2000). [ Intragenic complementation and the structure and function of argininosuccinate lyase]. Cell Mol Life Sci 57 (11): 1637-51. . PMID 11092456
- [[|Yu B, Thompson GD, Yip P, Howell PL, Davidson AR, ]], () ({{{Month}}} 2001). [ Mechanisms for intragenic complementation at the human argininosuccinate lyase locus]. Biochemistry 40 (51): 15581-90. . PMID 11747433
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