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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1c3c

E.C. nameadenylosuccinate lyase
SpeciesThermotoga maritima (Bacteria)
E.C. Number (IntEnz) 4.3.2.2
CSA Homologues of 1c3cThere are 46 Homologs
CSA Entries With UniProtID Q9X0I0
CSA Entries With EC Number 4.3.2.2
PDBe Entry 1c3c
PDBSum Entry 1c3c
MACiE Entry M0080

Literature Report

IntroductionAdenylosuccinate lyase catalyses two similar but separate reactions in the de novo purine synthesis pathway. In the first reaction is converts 5-aminoimidazole-(N-succinylcarboxyamide) ribotide into 5-aminoimidazole-4-carboxyamide ribotide in the ninth step of the synthesis of inosine monophosphate. In the second reaction the enzyme converts adenylosuccinate into adenosine monophospate which occurs four steps after the first reaction. Adenylosuccinate lyase helps provide the majority of purine nucleotides required for DNA replication as well as playing a role in cellular metabolism as an enzyme in the purine nucleotide cycle. The purine nucleotide cycle controls both the amounts of available citric acid intermediates and the amount of free AMP. Mutations in the enzyme leads to severe clinical consequences including mental retardation with autistic features.
Mechansim
Reaction

Catalytic Sites for 1c3c

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ThrA140140macie:sideChain
HisA141141macie:sideChain
LysB268268macie:sideChain
GluB275275macie:sideChain

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
LysA268268macie:sideChain
GluA275275macie:sideChain
ThrB140140macie:sideChain
HisB141141macie:sideChain

Literature References

Notes:
Toth EA
The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway.
Structure 2000 8 163-174
PubMed: 10673438
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