Adenylosuccinate lyase

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

ADSL
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesADSL, AMPS, ASASE, ASL, adenylosuccinate lyase, Adenylosuccinate lyase
External IDsOMIM: 608222 MGI: 103202 HomoloGene: 12 GeneCards: ADSL
Orthologs
SpeciesHumanMouse
Entrez

158

11564

Ensembl

ENSG00000239900

ENSMUSG00000022407

UniProt

P30566

P54822

RefSeq (mRNA)

NM_000026
NM_001123378
NM_001317923
NM_001363840

NM_009634

RefSeq (protein)

NP_000017
NP_001116850
NP_001304852
NP_001350769

NP_033764

Location (UCSC)Chr 22: 40.35 – 40.39 MbChr 15: 80.83 – 80.86 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse
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
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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.

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