Adenylosuccinate lyase information

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Adenylosuccinate lyase
Adenylosuccinate lyase
	'The homotetrameric structure of ASL in Thermotoga maritima Domain 1 is in red, Domain 2 is in blue, Domain 3 is in yellow. This structure was inspired by a paper by Toth and Yeates
Identifiers
EC no.	4.3.2.2
CAS no.	9027-81-0
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
PMC
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ADSL
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2J91, 2VD6, 4FFX, 4FLC
Identifiers
Aliases	ADSL, AMPS, ASASE, ASL, adenylosuccinate lyase, Adenylosuccinate lyase
External IDs	OMIM: 608222; MGI: 103202; HomoloGene: 12; GeneCards: ADSL; OMA:ADSL - orthologs
Gene location (Human)
Chr.	Chromosome 22 (human)
End	40,390,463 bp
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)
End	80,855,147 bp
RNA expression pattern
	Top expressed in
	muscle of thigh; ; gastrocnemius muscle; ; skeletal muscle tissue; ; gonad; ; lymph node; ; islet of Langerhans; ; body of pancreas; ; smooth muscle tissue; ; stromal cell of endometrium; ; ventricular zone;
	Top expressed in
	muscle of thigh; ; plantaris muscle; ; soleus muscle; ; extensor digitorum longus muscle; ; skeletal muscle tissue; ; extraocular muscle; ; triceps brachii muscle; ; tibialis anterior muscle; ; sternocleidomastoid muscle; ; ventricular zone;
	More reference expression data
	n/a
Gene ontology
Molecular function	N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity; catalytic activity; lyase activity;
Cellular component	cytosol;
Biological process	purine nucleotide biosynthetic process; purine ribonucleotide biosynthetic process; 'de novo' IMP biosynthetic process; purine ribonucleoside monophosphate biosynthetic process; 'de novo' AMP biosynthetic process; response to hypoxia; purine nucleotide metabolic process; AMP biosynthetic process; response to nutrient; aerobic respiration; ribonucleoside monophosphate biosynthetic process; response to muscle activity; response to starvation; protein tetramerization; metabolism;
	Sources:Amigo / QuickGO
Orthologs
	158
	11564
	ENSG00000239900
	ENSMUSG00000022407
	P30566
	P54822
	NM_000026; NM_001123378; NM_001317923; NM_001363840
	NM_009634
	NP_000017; NP_001116850; NP_001304852; NP_001350769
	NP_033764
	Wikidata
View/Edit Human	View/Edit Mouse

Adenylosuccinate lyase (or adenylosuccinase) is an enzyme that in humans is encoded by the ADSL gene.^[6]

Adenylosuccinate lyase converts adenylosuccinate to AMP and fumarate as part of the purine nucleotide cycle. ASL catalyzes two reactions in the purine biosynthetic pathway that makes AMP; ASL cleaves adenylosuccinate into AMP and fumarate, and cleaves SAICAR into AICAR and fumarate.

Adenylosuccinate lyase is part of the β-elimination superfamily of enzymes and it proceeds through an E1cb reaction mechanism. The enzyme is a homotetramer with three domains in each monomer and four active sites per homotetramer.

Point mutations in adenylosuccinate that cause lowered enzymatic activity cause clinical symptoms that mark the condition adenylosuccinate lyase deficiency.

This protein may use the morpheein model of allosteric regulation.^[7]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000239900 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000022407 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Toth EA, Yeates TO (February 2000). "The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway". Structure. 8 (2): 163–74. doi:10.1016/S0969-2126(00)00092-7. PMID 10673438.
^ "Entrez Gene: Adenylosuccinate lyase". Retrieved 2012-03-01.
^ Selwood T, Jaffe EK (Mar 2012). "Dynamic dissociating homo-oligomers and the control of protein function". Archives of Biochemistry and Biophysics. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000239900 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000022407 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10673438-5] Toth EA, Yeates TO (February 2000). "The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway". Structure. 8 (2): 163–74. doi:10.1016/S0969-2126(00)00092-7. PMID 10673438.

[entrez-6] "Entrez Gene: Adenylosuccinate lyase". Retrieved 2012-03-01.

[pmid22182754-7] Selwood T, Jaffe EK (Mar 2012). "Dynamic dissociating homo-oligomers and the control of protein function". Archives of Biochemistry and Biophysics. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.

Adenylosuccinate lyase information

and 18 Related for: Adenylosuccinate lyase information

Adenylosuccinate lyase

Adenylosuccinate lyase deficiency

Adenylosuccinate

Purine metabolism

Brachycephaly

Angelman syndrome

Nucleotide

Bacillus subtilis

Anaplerotic reactions

Fumarate lyase

List of genetic disorders

Causes of autism

Purine nucleotide cycle

Morpheein

SAICA

Purinosome

GMP synthase

GABPB2