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Overview for MACiE Entry M0151

Version history

General Information

EC Number: 2.7.6.3 (A member of the Transferases, Transferring phosphorus-containing groups, Diphosphotransferases)

Enzyme Name: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase

Biological Species: Escherichia coli (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

  • P26281 - 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase

Representative PDB Code: 1q0n - CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE FROM E. COLI WITHMGAMPCPP AND 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN AT 1.25ANGSTROM RESOLUTION (Resolution = 1.25 Å).

Catalytic CATH Codes:

Display structure information

Overall Reaction:

Image of ATP

Image of 6-hydroxymethyl-7,8-dihydropterin

right arrow

Image of 7,8-dihydro-6-(diphosphooxymethyl)pterin

Image of AMP

Image of proton

ATP
C00002
CHEBI:30616
6-hydroxymethyl-7,8-dihydropterin
C01300
CHEBI:17083
7,8-dihydro-6-(diphosphooxymethyl)pterin
C04807
CHEBI:15998
AMP
C00020
CHEBI:456215
proton
C00080
CHEBI:15378
CHEBI:24636

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Stepwise Description of the Reaction

Step 1Water deprotonates the alcohol group of 6-hydroxymethyl-7,8-dihydropterin, which in turn attacks the beta phosphate of the ATP in a nucelophilic substitution reaction that generates the 7,8-dihydro-6-(diphosphooxymethyl)pterin and AMP products

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Arg 82 A Side Chain
Arg 92 A Side Chain

Metal Cofactors for M0151

Type Het group Number Chain
magnesium MG 161 x Overview
magnesium MG 162 x Overview

References

  1. J. Blaszczyk et al. (2000), Structure, 8, 1049-1058. Catalytic center assembly of HPPK as revealed by the crystal structure of a ternary complex at 1.25 A resolution.
    Medline: 11080626
  2. Y. Li et al. (2005), Biochemistry, 44, 8590-8599. Is the critical role of loop 3 of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase in catalysis due to loop-3 residues arginine-84 and tryptophan-89? Site-directed mutagenesis, biochemical, and crystallographic studies.
    Medline: 15952765

Homologue information for M0151 (1q0n)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)


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

GOA logo
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity (molecular function)
folic acid-containing compound biosynthetic process (biological process)
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