2.4.2.57: AMP phosphorylase
This is an abbreviated version!
For detailed information about AMP phosphorylase, go to the full flat file.
Word Map on EC 2.4.2.57
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2.4.2.57
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thermococcus
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cardiac
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ribose-1,5-bisphosphate
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amines
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rubiscos
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norepinephrine
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contractile
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kodakarensis
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glucagon
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isoproterenol
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1,5-bisphosphate
- 2.4.2.57
-
thermococcus
- cardiac
-
ribose-1,5-bisphosphate
- amines
- rubiscos
- norepinephrine
-
contractile
- kodakarensis
- glucagon
- isoproterenol
- 1,5-bisphosphate
Reaction
Synonyms
AMPpase, deoA, nucleoside monophosphate phosphorylase
ECTree
2.4.2.57 AMP phosphorylaseAdvanced search results
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Subunits on EC 2.4.2.57 - AMP phosphorylase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
multimer
forms a large macromolecular structure of more than 40 subunits in solution. Structures of two truncated forms of Tk-AMPpase (Tk-AMPpaseDELTAN84 and Tk-AMPpaseDELTAC10) clarify that the multimerization is achieved by two dimer interfaces within a single molecule: one by the central domain and the other by the C-terminal domain, which consists of an unexpected domain-swapping interaction. The N-terminal domain, characteristic of archaeal enzymes, is essential for enzymatic activity, participating in multimerization as well as domain closure of the active site upon substrate binding. Biochemical analysis demonstrates that the macromolecular assembly of the enzyme contributes to its high thermostability
