6.3.2.12: dihydrofolate synthase

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

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]

Systematic Name

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Systematic Name on EC 6.3.2.12 - dihydrofolate synthase

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SYSTEMATIC NAME

IUBMB Comments

7,8-dihydropteroate:L-glutamate ligase (ADP-forming)

In some bacteria, a single protein catalyses both this activity and that of EC 6.3.2.17, tetrahydrofolate synthase [2], the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H4PteGlun), i.e. various tetrahydrofolates. In contrast, the activities are located on separate proteins in most eukaryotes studied to date [3]. This enzyme is reponsible for attaching the first glutamate residue to dihydropteroate to form dihydrofolate and is present only in those organisms that have the ability to synthesize tetrahydrofolate de novo, e.g. plants, most bacteria, fungi and protozoa [3].