Dihydrofolic acid - Revision history

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Marked this version for translation

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	{{Short description\|Class of enzymes}}		{{Short description\|Class of enzymes}}
	{{infobox enzyme		{{infobox enzyme
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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-->

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	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 = 310–6 \| 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 = 310–6 \| 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 = 5625–30 \| 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 = 5625–30 \| 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 = 437–52 \| 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 = 437–52 \| 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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	{{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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Fire: Created page with " {{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..."

2024-04-05T06:59:33Z

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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<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 [[catalysis|catalyzes]] the [[chemical reaction]]

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

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==

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==
* {{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 = 310–6 | 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 = 5625–30 | pmid = 2985605 | issue = 9 | doi = 10.1016/S0021-9258(18)89069-X | doi-access = free }}
* {{cite journal | author = R, Rebeille F | date = 2001 | title = Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 98 | pages = 15360–5 | pmid = 11752472 | doi = 10.1073/pnas.261585098 | last2 = Cherest | first2 = H | last3 = Jabrin | first3 = S | last4 = Grunwald | first4 = D | last5 = Surdin-Kerjan | first5 = Y | last6 = Douce | first6 = R | last7 = Rébeillé | first7 = F | issue = 26 | pmc = 65034 | bibcode = 2001PNAS...9815360R | doi-access = free }}
* {{cite journal | vauthors = Cherest H, Thomas D, Surdin-Kerjan Y | date = 2000 | title = Polyglutamylation of folate coenzymes is necessary for methionine biosynthesis and maintenance of intact mitochondrial genome in Saccharomyces cerevisiae | journal = J. Biol. Chem. | volume = 275 | pages = 14056–63 | pmid = 10799479 | doi = 10.1074/jbc.275.19.14056 | issue = 19 | doi-access = free }}
* {{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 = 437–52 | pmid = 9190084 | doi = 10.1016/S0031-9422(96)00833-3 | issue = 3 }}

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

{{二次利用|date=26 August 2023}}
[[Category:EC 6.3.2]]
[[Category:Enzymes of known structure]]
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