6.3.2.12: dihydrofolate synthase

This is an abbreviated version!
For detailed information about dihydrofolate synthase, go to the full flat file.

Word Map on EC 6.3.2.12

6.3.2.12

tetrahydrofolate

polyglutamylated

analysis

medicine

drug development

biotechnology

Reaction

Synonyms

7,8-Dihydrofolate synthetase, 7,8-Dihydropteroate:L-glutamate ligase (ADP), DHFR, DHFS, dihydrofolate reductase, dihydrofolate synthase, Dihydrofolate synthetase, dihydrofolate synthetase-folylpolyglutamate synthetase, dihydropteroate:L-glutamate ligase (ADP-forming), FHFS, FHFS/FPGS, FolC, Folylpoly-(gamma-glutamate) synthetase-dihydrofolate synthase, Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase, H2-folate synthetase, LH57_13380, PfDHFS-FPGS, PNEJI1_000945, Rv2447c, Synthetase, dihydrofolate

ECTree

6 Ligases

6.3 Forming carbon-nitrogen bonds

6.3.2 Acid—amino-acid ligases (peptide synthases)

6.3.2.12 dihydrofolate synthase

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Results	in table
15632	AA Sequence
8	Application
1	CAS Registry Number
13	Cloned(Commentary)
3	Cofactor
1	Crystallization (Commentary)
1	Expression
11	General Information
2	General Stability
1	IC50 Value
35	Inhibitors
3	Ki Value [mM]
26	KM Value [mM]
9	Localization
38	Metals/Ions
8	Molecular Weight [Da]
7	Natural Substrates/ Products (Substrates)
402	Organism
6	Pathway
5	PDB ID
6	pH Optimum
3	pH Range
60	Protein Variants
12	Purification (Commentary)
1	Reaction
2	Reaction Type
51	Reference
4	Source Tissue
7	Specific Activity [micromol/min/mg]
4	Storage Stability
57	Substrates and Products (Substrate)
4	Subunits
43	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Temperature Stability [°C]

KM Value

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KM Value on EC 6.3.2.12 - dihydrofolate synthase

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0.00025 - 0.035

7,8-dihydropteroate

6 entries

0.0029 - 0.29

ATP

8 entries

0.00088

dihydropteroate

2 entries

1.5 - 3.9

Glu

3 entries

0.00597

glutamate

Plasmodium falciparum

705610

0.006 - 9.1

L-Glu

5 entries

additional information

Plasmodium falciparum

non-standard kinetics at high glutamate and ATP concentrations, being partially inhibited by increasing concentrations of its principal substrate, dihydropteroate. Binding of dihydropteroate to the catalytic and inhibitory sites exhibits dissociation constants of 0.50 microM and 1.25 microM, respectively. Under lower co-substrate concentrations, data fit the Michaelis-Menten equation

705610