2.7.6.3: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
This is an abbreviated version!
For detailed information about 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase, go to the full flat file.
Word Map on EC 2.7.6.3
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2.7.6.3
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pyrophosphorylation
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pyrophosphate
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pterins
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folic
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dihydrofolate
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bisubstrate
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sulfa
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dihydroneopterin
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ampcpp
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tetrahydrofolate
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induced-fit
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drug development
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medicine
- 2.7.6.3
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pyrophosphorylation
- pyrophosphate
- pterins
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folic
- dihydrofolate
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bisubstrate
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sulfa
- dihydroneopterin
- ampcpp
- tetrahydrofolate
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induced-fit
- drug development
- medicine
Reaction
Synonyms
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase, 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase, 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase/dihydropteroate synthase, 6-hydroxy-7,8-dihydropterin pyrophosphokinase, 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK), 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase-dihydropteroate synthase, 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/dihydropteroate synthase, 6-hydroxymethyl-7,8-dihydroxypterin pyrophosphokinase/7,8-dihydropteroate synthase, 6-hydroxymethylpterin pyrophosphokinase, 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase, 7,8-dihydropteroate-synthesizing enzyme, 7,8-dihydroxymethylpterin-pyrophosphokinase, ATP:2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine 6'-pyrophosphotransferase, cytHPPK/DHPS, dihydropterin pyrophosphokinase, FOLK, FtHPPK-DHPS, H2-pteridine-CH2-OH pyrophosphokinase, H2-pteridine-CH2OH pyrophosphokinase, HPPK, HPPK-DHPS, HPPK/DHPS, HPPK/dihydropteroate synthase, hydroxymethyl-7,8-dihydropterin pyrophosphokinase/7,8-dihydropteroate synthase, hydroxymethyldihydropteridine pyrophosphokinase, hydroxymethyldihydropterin diphosphokinase/dihydropteroate synthase, hydroxymethyldihydropterin pyrophosphokinase (HPPK), hydroxymethyldihydropterin pyrophosphokinase-dihydropteroate synthase, mitHPPK/DHPS, More, PPPK, PPPK-DHPS, PVX_123230, pyrophosphokinase, 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine
ECTree
2.7.6.3 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinaseAdvanced search results
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Engineering on EC 2.7.6.3 - 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
R82A
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mutation causes a decrease in the rate constant for the chemical step by a factor of 380, no significant change in the binding energy or kinetics of either substrate
R84A
R92A
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mutation causes a decrease in the rate constant for the chemical step by a factor of 35000. The mutation causes no significant change in the binding energy or binding kinetics of MgATP2-. It does not cause a significant change in the binding energy of 6-hydroxymethyl-7,8-dihydropterin either but causes a decrease in the association rate constant for the binding of 6-hydroxymethyl-7,8-dihydropterin by a factor of 1.4 and a decrease in the dissociation rate constant by a factor of 10
V83Gdel84-89
the deletion mutation does not have significant effects on the dissociation constants or the rate constants for the binding of the first substrate MgATP2- or its analogues. The dissociation constant of 6-hydroxymethyl-7,8-dihydropterin for the mutant increases by a factor of about 100, which is due to a large increase in the dissociation rate constant. The deletion mutation causes a shift of the rate-limiting step in the reaction and a decrease in the rate constant for the chemical step by a factor of 110000. The crystal structures reveal that the deletion mutation does not affect protein folding, but the catalytic center of the mutant is not fully assembled even upon the formation of the ternary complex and is not properly sealed. Loop 3 is dispensable for the folding of the protein and the binding of the first substrate MgATP2-, but is required for the assembling and sealing of the active center. The loop plays an important role in the stabilization of the ternary complex and is critical for catalysis
W89A
S436A/A437G
1.6fold increase in kcat/Km value for 4-aminobenzoate
S436F/A437G/A613S
2fold increase in kcat/Km value of 4-aminobenzoate
A383G
A553G
K512D
K512E
S382A
V585A
additional information
R84A
little changes in the dissociation constants and kinetic constants of the HPPK-catalyzed reaction
R84A
the mutation causes little changes in either dissociation constants or kinetic constants of the enzyme-catalyzed reaction except that the rate constant for the chemical step of the forward reaction decreases by a factor of 4
W89A
mutation increases the Kd for the binding of MgATP2- by a factor of 3, whereas the Kd for 6-hydroxymethyl-7,8-dihydropterin increases by a factor of 6, which is due to the increase in the dissociation rate constant. The mutation decreases the rate constant for the chemical step of the forward reaction by a factor of 15 and the rate constant for the chemical step of the reverse reaction by a factor of 25. The crystal structures of W89A show that W89A has different conformations in loops 2 and 3, but the critical catalytic residues are positioned for catalysis
W89A
the mutation does not have any significant effects on the Kd and the rate constants for the binding of MgATP, but the Kd for 6-hydroxymethyl-7,8-dihydropteridine of the mutant increases by a factor of 6.5. The mutation decreases the rate constant for the chemical step of the forward reaction by a factor of about 23 and the rate constant for the chemical step of the reverse reaction by a factor of about 33
A383G
dominant drug resistance mutation. Mutation subtly alters the intricate enzyme-4-amino benzoic acid-sulfadoxine interactions such that DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
A383G
natural mutation, generates resistance to sulfadoxine. DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
A553G
dominant drug resistance mutation. Mutation subtly alters the intricate enzyme-4-amino benzoic acid-sulfadoxine interactions such that DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
A553G
natural mutation, generates resistance to sulfadoxine. DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
K512D
dominant drug resistance mutation. Mutation subtly alters the intricate enzyme-4-amino benzoic acid-sulfadoxine interactions such that DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
K512D
natural mutation, generates resistance to sulfadoxine. DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
K512E
dominant drug resistance mutation. Mutation subtly alters the intricate enzyme-4-amino benzoic acid-sulfadoxine interactions such that DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
K512E
natural mutation, generates resistance to sulfadoxine. DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
S382A
dominant drug resistance mutation. Mutation subtly alters the intricate enzyme-4-amino benzoic acid-sulfadoxine interactions such that DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
S382A
natural mutation, generates resistance to sulfadoxine. DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
V585A
dominant drug resistance mutation. Mutation subtly alters the intricate enzyme-4-amino benzoic acid-sulfadoxine interactions such that DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
V585A
natural mutation, generates resistance to sulfadoxine. DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
additional information
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construction of a T-DNA insertion mutant in the cytHPPK/DHPS gene, resulting in lower germination rates as compared with the wild-type upon application of oxidative and osmotic stress, phenotype, overview
additional information
construction of a T-DNA insertion mutant in the cytHPPK/DHPS gene, resulting in lower germination rates as compared with the wild-type upon application of oxidative and osmotic stress, phenotype, overview
additional information
the enzyme is minimally biotinylated by reaction with EZ-Link sulfo-NHS-LC-LC-biotin
