Dihydrofolic acid: Difference between revisions

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Created page with "<languages /> <translate> {{Short description|Class of enzymes}} {{infobox enzyme | Name = Dihydrofolate synthase | EC_number = 6.3.2.12 | CAS_number = 37318-62-0 | GO_code = 0008841 | image = 1w7k.jpg | width = 270 | caption = Dihydrofolate synthase monomer, E.Coli }} In enzymology, a '''dihydrofolate synthase''' ({{EnzExplorer|6.3.2.12}}) is an enzyme that catalyzes the chemical reaction :ATP + 7,8-dihydropteroate + L-g..."
 
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{{Short description|Class of enzymes}}
{{Short description|Class of enzymes}}
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In [[enzymology]], a '''dihydrofolate synthase''' ({{EnzExplorer|6.3.2.12}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
In [[enzymology]], a '''dihydrofolate synthase''' ({{EnzExplorer|6.3.2.12}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]


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:ATP + 7,8-dihydropteroate + L-glutamate <math>\rightleftharpoons</math> ADP + phosphate + 7,8-dihydropteroylglutamate
:ATP + 7,8-dihydropteroate + L-glutamate <math>\rightleftharpoons</math> ADP + phosphate + 7,8-dihydropteroylglutamate


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The 3 [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]], [[7,8-dihydropteroate]], and [[L-glutamate]], whereas its 3 [[product (chemistry)|products]] are [[adenosine diphosphate|ADP]], [[phosphate]], and [[7,8-dihydropteroylglutamate]].
The 3 [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]], [[7,8-dihydropteroate]], and [[L-glutamate]], whereas its 3 [[product (chemistry)|products]] are [[adenosine diphosphate|ADP]], [[phosphate]], and [[7,8-dihydropteroylglutamate]].


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This enzyme belongs to the family of [[ligase]]s, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases).  The [[List of enzymes|systematic name]] of this enzyme class is '''7,8-dihydropteroate:L-glutamate ligase (ADP-forming)'''. Other names in common use include '''dihydrofolate synthetase''', '''7,8-dihydrofolate synthetase''', '''H2-folate synthetase''', '''7,8-dihydropteroate:L-glutamate ligase (ADP)''', '''dihydrofolate synthetase-folylpolyglutamate synthetase''', '''folylpoly-(gamma-glutamate) synthetase-dihydrofolate synthase''', '''FHFS''', '''FHFS/FPGS''', '''dihydropteroate:L-glutamate ligase (ADP-forming)''', and '''DHFS'''.  This enzyme participates in [[folate biosynthesis]].
This enzyme belongs to the family of [[ligase]]s, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases).  The [[List of enzymes|systematic name]] of this enzyme class is '''7,8-dihydropteroate:L-glutamate ligase (ADP-forming)'''. Other names in common use include '''dihydrofolate synthetase''', '''7,8-dihydrofolate synthetase''', '''H2-folate synthetase''', '''7,8-dihydropteroate:L-glutamate ligase (ADP)''', '''dihydrofolate synthetase-folylpolyglutamate synthetase''', '''folylpoly-(gamma-glutamate) synthetase-dihydrofolate synthase''', '''FHFS''', '''FHFS/FPGS''', '''dihydropteroate:L-glutamate ligase (ADP-forming)''', and '''DHFS'''.  This enzyme participates in [[folate biosynthesis]].


==Structural studies==
==Structural studies== <!--T:5-->


<!--T:6-->
As of late 2007, 3 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1W78}}, {{PDB link|1W7K}}, and {{PDB link|2BMB}}.
As of late 2007, 3 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1W78}}, {{PDB link|1W7K}}, and {{PDB link|2BMB}}.


==References==
==References== <!--T:7-->
* {{cite journal | vauthors = GRIFFIN MJ, BROWN GM | title = The Biosynthesis of Folic Acid. III. Enzymatic Formation of Dihydrofolic Acid from Dihydropteroic Acid and of Tetrahydropteroylpolyglutamic Acid Compounds from Tetrahydrofolic Acid | date = 1964 | journal = J. Biol. Chem.  | volume = 239 | pages = 310&ndash;6  | doi = 10.1016/S0021-9258(18)51783-X | pmid = 14114858 | doi-access = free }}
* {{cite journal | vauthors = GRIFFIN MJ, BROWN GM | title = The Biosynthesis of Folic Acid. III. Enzymatic Formation of Dihydrofolic Acid from Dihydropteroic Acid and of Tetrahydropteroylpolyglutamic Acid Compounds from Tetrahydrofolic Acid | date = 1964 | journal = J. Biol. Chem.  | volume = 239 | pages = 310&ndash;6  | doi = 10.1016/S0021-9258(18)51783-X | pmid = 14114858 | doi-access = free }}
* {{cite journal | vauthors = Bognar AL, Osborne C, Shane B, Singer SC, Ferone R | date = 1985 | title = Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase Cloning and high expression of the Escherichia coli folC gene and purification and properties of the gene product | journal = J. Biol. Chem.  | volume = 260 | pages = 5625&ndash;30  | pmid = 2985605 | issue = 9 | doi = 10.1016/S0021-9258(18)89069-X | doi-access = free }}
* {{cite journal | vauthors = Bognar AL, Osborne C, Shane B, Singer SC, Ferone R | date = 1985 | title = Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase Cloning and high expression of the Escherichia coli folC gene and purification and properties of the gene product | journal = J. Biol. Chem.  | volume = 260 | pages = 5625&ndash;30  | pmid = 2985605 | issue = 9 | doi = 10.1016/S0021-9258(18)89069-X | doi-access = free }}
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* {{cite journal | vauthors = Cossins EA, Chen L | date = 1997 | title = Folates and one-carbon metabolism in plants and fungi | journal = [[Phytochemistry (journal)|Phytochemistry]]  | volume = 45 | pages = 437&ndash;52  | pmid = 9190084 | doi = 10.1016/S0031-9422(96)00833-3 | issue = 3 }}
* {{cite journal | vauthors = Cossins EA, Chen L | date = 1997 | title = Folates and one-carbon metabolism in plants and fungi | journal = [[Phytochemistry (journal)|Phytochemistry]]  | volume = 45 | pages = 437&ndash;52  | pmid = 9190084 | doi = 10.1016/S0031-9422(96)00833-3 | issue = 3 }}


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{{Ligases CO CS and CN}}
{{Ligases CO CS and CN}}
{{Enzymes}}
{{Enzymes}}
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{{Portal bar|Biology|border=no}}


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{{二次利用|date=26 August 2023}}
{{二次利用|date=26 August 2023}}
[[Category:EC 6.3.2]]
[[Category:EC 6.3.2]]
[[Category:Enzymes of known structure]]
[[Category:Enzymes of known structure]]
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Latest revision as of 16:17, 5 April 2024

Dihydrofolate synthase
Dihydrofolate synthase monomer, E.Coli
Identifiers
EC no.6.3.2.12
CAS no.37318-62-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a dihydrofolate synthase (EC 6.3.2.12) is an enzyme that catalyzes the chemical reaction

ATP + 7,8-dihydropteroate + L-glutamate ADP + phosphate + 7,8-dihydropteroylglutamate

The 3 substrates of this enzyme are ATP, 7,8-dihydropteroate, and L-glutamate, whereas its 3 products are ADP, phosphate, and 7,8-dihydropteroylglutamate.

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is 7,8-dihydropteroate:L-glutamate ligase (ADP-forming). Other names in common use include dihydrofolate synthetase, 7,8-dihydrofolate synthetase, H2-folate synthetase, 7,8-dihydropteroate:L-glutamate ligase (ADP), dihydrofolate synthetase-folylpolyglutamate synthetase, folylpoly-(gamma-glutamate) synthetase-dihydrofolate synthase, FHFS, FHFS/FPGS, dihydropteroate:L-glutamate ligase (ADP-forming), and DHFS. This enzyme participates in folate biosynthesis.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1W78, 1W7K, and 2BMB.

References