Overview for MACiE Entry M0101
EC Number: 188.8.131.52 (A member of the Hydrolases, Acting on acid anhydrides, In phosphorus-containing anhydrides)
Enzyme Name: bis(5'-adenosyl)-triphosphatase
Biological Species: Homo sapiens (Human)
Catalytic Chain UniprotKB Accession Codes:
- P49789 - Bis(5'-adenosyl)-triphosphatase
Representative PDB Code: 5fit - FHIT-SUBSTRATE ANALOG (Resolution = 2.30 Å).
Catalytic CATH Codes:
Display structure information
Overall Comment: Dinocleoside polyphoshate hydrolases require millimolar Mn(II) Mg(II) or Ca(II) for optimum activity and are inhibited by Ni(II) Zn(II) and Cd(II). The identity of the Mg has been arbitrarily assigned due to lack of Mg in the crystal structure.
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Stepwise Description of the Reaction
|Step 1||His96 attacks the alpha phosphate of the substrate in a nucleophilic attack which proceeds via a pentavalent transition state and results in the elimination of ADP.|
|Step 2||ADP deprotonates water, which attacks the phosphate of the covalently bound AMP, eliminating His96 and proceeding via a pentavalent transition state.|
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Catalytic Residues Involved
||Location of Function
Metal Cofactors for M0101
||MG(not in PDB)
- C. D. Lima et al. (1997), Science, 278, 286-290. Structure-based analysis of catalysis and substrate definition in the HIT protein family.
- C. Brenner et al. (1997), Nat. Struct. Biol., 4, 231-238. Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins.
- K. Huang et al. (2004), Biochemistry, 43, 7637-7642. The mechanism of action of the fragile histidine triad, Fhit: isolation of a covalent adenylyl enzyme and chemical rescue of H96G-Fhit.
Homologue information for M0101 (5fit)
MACiE Homologues (within the PDB)
MACiE Homologues (within UniprotKB/SwissProt)
Entries with at least one Catalytic CATH code in common (different mechanisms):
|M0088 ||UDP-glucose-hexose-1-phosphate uridylyltransferase |
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