Dihydrofolic acid: Difference between revisions
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--> | ||
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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}} | ||
{{Portal bar|Biology|border=no}} | {{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 | |||||||||
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![]() Dihydrofolate synthase monomer, E.Coli | |||||||||
Identifiers | |||||||||
EC no. | 6.3.2.12 | ||||||||
CAS no. | 37318-62-0 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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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
- GRIFFIN MJ, BROWN GM (1964). "The Biosynthesis of Folic Acid. III. Enzymatic Formation of Dihydrofolic Acid from Dihydropteroic Acid and of Tetrahydropteroylpolyglutamic Acid Compounds from Tetrahydrofolic Acid". J. Biol. Chem. 239: 310–6. doi:10.1016/S0021-9258(18)51783-X. PMID 14114858.
- Bognar AL, Osborne C, Shane B, Singer SC, Ferone R (1985). "Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase Cloning and high expression of the Escherichia coli folC gene and purification and properties of the gene product". J. Biol. Chem. 260 (9): 5625–30. doi:10.1016/S0021-9258(18)89069-X. PMID 2985605.
- R, Rebeille F; Cherest, H; Jabrin, S; Grunwald, D; Surdin-Kerjan, Y; Douce, R; Rébeillé, F (2001). "Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana". Proc. Natl. Acad. Sci. U.S.A. 98 (26): 15360–5. Bibcode:2001PNAS...9815360R. doi:10.1073/pnas.261585098. PMC 65034. PMID 11752472.
- Cherest H, Thomas D, Surdin-Kerjan Y (2000). "Polyglutamylation of folate coenzymes is necessary for methionine biosynthesis and maintenance of intact mitochondrial genome in Saccharomyces cerevisiae". J. Biol. Chem. 275 (19): 14056–63. doi:10.1074/jbc.275.19.14056. PMID 10799479.
- Cossins EA, Chen L (1997). "Folates and one-carbon metabolism in plants and fungi". Phytochemistry. 45 (3): 437–52. doi:10.1016/S0031-9422(96)00833-3. PMID 9190084.
![]() | この記事は、クリエイティブ・コモンズ・表示・継承ライセンス3.0のもとで公表されたウィキペディアの項目Dihydrofolic acid(26 August 2023編集記事参照)を素材として二次利用しています。 Item:Q21788 ![]() |