spacer

Overview for MACiE Entry M0101

Version history

General Information

EC Number: 3.6.1.29 (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 Reaction:

Image of P1,P3-Bis(5'-adenosyl) triphosphate

Image of water

right arrow

Image of ADP

Image of AMP

P1,P3-Bis(5'-adenosyl) triphosphate
C06197
CHEBI:58529
water
C00001
CHEBI:15377
ADP
C00008
CHEBI:16761
AMP
C00020
CHEBI:16027

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.


View similar reactions


Stepwise Description of the Reaction

Step 1His96 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 2ADP deprotonates water, which attacks the phosphate of the covalently bound AMP, eliminating His96 and proceeding via a pentavalent transition state.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Gln 83 A Side Chain
His 96 A Side Chain
His 98 A Side Chain

Metal Cofactors for M0101

Type Het group Number Chain
magnesium MG(not in PDB) 1 x Overview

References

  1. C. D. Lima et al. (1997), Science, 278, 286-290. Structure-based analysis of catalysis and substrate definition in the HIT protein family.
    Medline: 9323207
  2. 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.
    Medline: 9164465
  3. 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.
    Medline: 15182206

Homologue information for M0101 (5fit)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)



Entries with at least one Catalytic CATH code in common (different mechanisms):

MACiE Entry Enzyme Name
EC Number
PDB code CATH code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0088 UDP-glucose-hexose-1-phosphate uridylyltransferase
2.7.7.12
1hxq 3.30.428.10
0.750.6500Compare

Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ
Link to EzCatDB

GOA logo
catalytic activity (molecular function)
protein binding (molecular function)
nucleus (cellular component)
cytoplasm (cellular component)
cytosol (cellular component)
plasma membrane (cellular component)
DNA replication (biological process)
nucleotide metabolic process (biological process)
diadenosine triphosphate catabolic process (biological process)
nickel cation binding (molecular function)
hydrolase activity (molecular function)
intracellular membrane-bounded organelle (cellular component)
bis(5'-adenosyl)-triphosphatase activity (molecular function)
spacer
spacer