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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''C-1-tetrahydrofolate synthase, cytoplasmic''' also known as '''C1-THF synthase''' is an [[enzyme]] that in humans is encoded by the ''MTHFD1'' ('''m'''ethylenete'''t'''ra'''h'''ydro'''f'''olate '''d'''ehydrogenase '''1''') [[gene]].<ref name="pmid3053686">{{cite journal |vauthors=Hum DW, Bell AW, Rozen R, MacKenzie RE | title = Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase | journal = J Biol Chem | volume = 263 | issue = 31 | pages = 15946–50 |date=Dec 1988 | pmid = 3053686 | pmc =  | doi =  }}</ref><ref name="pmid2786332">{{cite journal |vauthors=Rozen R, Barton D, Du J, Hum DW, MacKenzie RE, Francke U | title = Chromosomal localization of the gene for the human trifunctional enzyme, methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase | journal = Am J Hum Genet | volume = 44 | issue = 6 | pages = 781–6 |date=Jun 1989 | pmid = 2786332 | pmc = 1715669 | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MTHFD1 methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 1, methenyltetrahydrofolate cyclohydrolase, formyltetrahydrofolate synthetase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4522| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_MTHFD1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a4i.
| PDB = {{PDB2|1a4i}}, {{PDB2|1dia}}, {{PDB2|1dib}}, {{PDB2|1dig}}
| Name = Methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 1, methenyltetrahydrofolate cyclohydrolase, formyltetrahydrofolate synthetase
| HGNCid = 7432
| Symbol = MTHFD1
| AltSymbols =; MTHFC; MTHFD
| OMIM = 172460
| ECnumber = 
| Homologene = 55940
| MGIid = 1342005
| GeneAtlas_image1 = PBB_GE_MTHFD1_202309_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004329 |text = formate-tetrahydrofolate ligase activity}} {{GNF_GO|id=GO:0004477 |text = methenyltetrahydrofolate cyclohydrolase activity}} {{GNF_GO|id=GO:0004488 |text = methylenetetrahydrofolate dehydrogenase (NADP+) activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016155 |text = formyltetrahydrofolate dehydrogenase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016874 |text = ligase activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0000105 |text = histidine biosynthetic process}} {{GNF_GO|id=GO:0006164 |text = purine nucleotide biosynthetic process}} {{GNF_GO|id=GO:0006548 |text = histidine catabolic process}} {{GNF_GO|id=GO:0006730 |text = one-carbon compound metabolic process}} {{GNF_GO|id=GO:0008652 |text = amino acid biosynthetic process}} {{GNF_GO|id=GO:0009086 |text = methionine biosynthetic process}} {{GNF_GO|id=GO:0009396 |text = folic acid and derivative biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4522
    | Hs_Ensembl = ENSG00000100714
    | Hs_RefseqProtein = NP_005947
    | Hs_RefseqmRNA = NM_005956
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 63924821
    | Hs_GenLoc_end = 63996474
    | Hs_Uniprot = P11586
    | Mm_EntrezGene = 108156
    | Mm_Ensembl = ENSMUSG00000021048
    | Mm_RefseqmRNA = NM_138745
    | Mm_RefseqProtein = NP_620084
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 77174138
    | Mm_GenLoc_end = 77238642
    | Mm_Uniprot = Q3TW74
  }}
}}
'''Methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 1, methenyltetrahydrofolate cyclohydrolase, formyltetrahydrofolate synthetase''', also known as '''MTHFD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MTHFD1 methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 1, methenyltetrahydrofolate cyclohydrolase, formyltetrahydrofolate synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4522| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes a protein that possesses three distinct enzymatic activities, [[methylenetetrahydrofolate dehydrogenase (NADP+)|methylenetetrahydrofolate dehydrogenase]] (1.5.1.5), [[methenyltetrahydrofolate cyclohydrolase]] (3.5.4.9) and [[formate–tetrahydrofolate ligase]] (6.3.4.3). Each of these activities catalyzes one of three sequential reactions in the interconversion of 1-carbon derivatives of [[tetrahydrofolic acid|tetrahydrofolate]], which are substrates for [[methionine]], [[thymidine monophosphate|thymidylate]], and de novo [[purine]] syntheses. The trifunctional enzymatic activities are conferred by two major domains, an aminoterminal portion containing the dehydrogenase and cyclohydrolase activities and a larger synthetase domain.<ref name="entrez"/><ref name="pmid21813566">{{cite journal |vauthors=Watkins D, Schwartzentruber JA, Ganesh J, Orange JS, Kaplan BS, Nunez LD, Majewski J, Rosenblatt DS | title = Novel inborn error of folate metabolism: identification by exome capture and sequencing of mutations in the MTHFD1 gene in a single proband | journal = J. Med. Genet. | volume = 48 | issue = 9 | pages = 590–2 |date=September 2011 | pmid = 21813566 | doi = 10.1136/jmedgenet-2011-100286  }}</ref>
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a protein that possesses three distinct enzymatic activities, 5,10-methylenetetrahydrofolate dehydrogenase, 5,10-methenyltetrahydrofolate cyclohydrolase and 10-formyltetrahydrofolate synthetase. Each of these activities catalyzes one of three sequential reactions in the interconversion of 1-carbon derivatives of tetrahydrofolate, which are substrates for methionine, thymidylate, and de novo purine syntheses. The trifunctional enzymatic activities are conferred by two major domains, an aminoterminal portion containing the dehydrogenase and cyclohydrolase activities and a larger synthetase domain.<ref name="entrez">{{cite web | title = Entrez Gene: MTHFD1 methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 1, methenyltetrahydrofolate cyclohydrolase, formyltetrahydrofolate synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4522| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal   |vauthors=Schild D, Brake AJ, Kiefer MC, etal |title=Cloning of three human multifunctional de novo purine biosynthetic genes by functional complementation of yeast mutations. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 8 |pages= 2916–20 |year= 1990 |pmid= 2183217 |doi=10.1073/pnas.87.8.2916 | pmc=53804  }}
| citations =
*{{cite journal  |vauthors=Peri KG, Belanger C, Mackenzie RE |title=Nucleotide sequence of the human NAD-dependent methylene tetrahydrofolate dehydrogenase-cyclohydrolase. |journal=Nucleic Acids Res. |volume=17 |issue= 21 |pages= 8853 |year= 1989 |pmid= 2587219 |doi=10.1093/nar/17.21.8853  | pmc=335047 }}
*{{cite journal | author=Schild D, Brake AJ, Kiefer MC, ''et al.'' |title=Cloning of three human multifunctional de novo purine biosynthetic genes by functional complementation of yeast mutations. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 8 |pages= 2916-20 |year= 1990 |pmid= 2183217 |doi=  }}
*{{cite journal  |vauthors=MacKenzie RE, Mejia N, Yang XM |title=Methylenetetrahydrofolate dehydrogenases in normal and transformed mammalian cells. |journal=Adv. Enzyme Regul. |volume=27 |issue= |pages= 31–9 |year= 1989 |pmid= 3074630 |doi=  10.1016/0065-2571(88)90007-6}}
*{{cite journal  | author=Peri KG, Belanger C, Mackenzie RE |title=Nucleotide sequence of the human NAD-dependent methylene tetrahydrofolate dehydrogenase-cyclohydrolase. |journal=Nucleic Acids Res. |volume=17 |issue= 21 |pages= 8853 |year= 1989 |pmid= 2587219 |doi=  }}
*{{cite journal  |vauthors=Shannon KW, Rabinowitz JC |title=Purification and characterization of a mitochondrial isozyme of C1-tetrahydrofolate synthase from Saccharomyces cerevisiae. |journal=J. Biol. Chem. |volume=261 |issue= 26 |pages= 12266–71 |year= 1986 |pmid= 3528153 |doi=  }}
*{{cite journal  | author=Rozen R, Barton D, Du J, ''et al.'' |title=Chromosomal localization of the gene for the human trifunctional enzyme, methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase. |journal=Am. J. Hum. Genet. |volume=44 |issue= 6 |pages= 781-6 |year= 1989 |pmid= 2786332 |doi=  }}
*{{cite journal  |vauthors=Mejia NR, MacKenzie RE |title=NAD-dependent methylenetetrahydrofolate dehydrogenase is expressed by immortal cells. |journal=J. Biol. Chem. |volume=260 |issue= 27 |pages= 14616–20 |year= 1985 |pmid= 3877056 |doi=  }}
*{{cite journal  | author=Hum DW, Bell AW, Rozen R, MacKenzie RE |title=Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase. |journal=J. Biol. Chem. |volume=263 |issue= 31 |pages= 15946-50 |year= 1988 |pmid= 3053686 |doi=  }}
*{{cite journal  |vauthors=Allaire M, Li Y, MacKenzie RE, Cygler M |title=The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 A resolution. |journal=Structure |volume=6 |issue= 2 |pages= 173–82 |year= 1998 |pmid= 9519408 |doi=10.1016/S0969-2126(98)00019-7 }}
*{{cite journal  | author=MacKenzie RE, Mejia N, Yang XM |title=Methylenetetrahydrofolate dehydrogenases in normal and transformed mammalian cells. |journal=Adv. Enzyme Regul. |volume=27 |issue= |pages= 31-9 |year= 1989 |pmid= 3074630 |doi=  }}
*{{cite journal   |vauthors=Hol FA, van der Put NM, Geurds MP, etal |title=Molecular genetic analysis of the gene encoding the trifunctional enzyme MTHFD (methylenetetrahydrofolate-dehydrogenase, methenyltetrahydrofolate-cyclohydrolase, formyltetrahydrofolate synthetase) in patients with neural tube defects. |journal=Clin. Genet. |volume=53 |issue= 2 |pages= 119–25 |year= 1998 |pmid= 9611072 |doi=10.1111/j.1399-0004.1998.tb02658.x  }}
*{{cite journal  | author=Shannon KW, Rabinowitz JC |title=Purification and characterization of a mitochondrial isozyme of C1-tetrahydrofolate synthase from Saccharomyces cerevisiae. |journal=J. Biol. Chem. |volume=261 |issue= 26 |pages= 12266-71 |year= 1986 |pmid= 3528153 |doi=  }}
*{{cite journal   |vauthors=Schmidt A, Wu H, MacKenzie RE, etal |title=Structures of three inhibitor complexes provide insight into the reaction mechanism of the human methylenetetrahydrofolate dehydrogenase/cyclohydrolase. |journal=Biochemistry |volume=39 |issue= 21 |pages= 6325–35 |year= 2000 |pmid= 10828945 |doi=10.1021/bi992734y }}
*{{cite journal | author=Mejia NR, MacKenzie RE |title=NAD-dependent methylenetetrahydrofolate dehydrogenase is expressed by immortal cells. |journal=J. Biol. Chem. |volume=260 |issue= 27 |pages= 14616-20 |year= 1985 |pmid= 3877056 |doi= }}
*{{cite journal   |vauthors=Brody LC, Conley M, Cox C, etal |title=A polymorphism, R653Q, in the trifunctional enzyme methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase/formyltetrahydrofolate synthetase is a maternal genetic risk factor for neural tube defects: report of the Birth Defects Research Group. |journal=Am. J. Hum. Genet. |volume=71 |issue= 5 |pages= 1207–15 |year= 2003 |pmid= 12384833 |doi=10.1086/344213  | pmc=385099 }}
*{{cite journal | author=Allaire M, Li Y, MacKenzie RE, Cygler M |title=The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 A resolution. |journal=Structure |volume=6 |issue= 2 |pages= 173-82 |year= 1998 |pmid= 9519408 |doi=  }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Hol FA, van der Put NM, Geurds MP, ''et al.'' |title=Molecular genetic analysis of the gene encoding the trifunctional enzyme MTHFD (methylenetetrahydrofolate-dehydrogenase, methenyltetrahydrofolate-cyclohydrolase, formyltetrahydrofolate synthetase) in patients with neural tube defects. |journal=Clin. Genet. |volume=53 |issue= 2 |pages= 119-25 |year= 1998 |pmid= 9611072 |doi=  }}
*{{cite journal   |vauthors=Gevaert K, Goethals M, Martens L, etal |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566–9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
*{{cite journal | author=Schmidt A, Wu H, MacKenzie RE, ''et al.'' |title=Structures of three inhibitor complexes provide insight into the reaction mechanism of the human methylenetetrahydrofolate dehydrogenase/cyclohydrolase. |journal=Biochemistry |volume=39 |issue= 21 |pages= 6325-35 |year= 2000 |pmid= 10828945 |doi=  }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
*{{cite journal | author=Brody LC, Conley M, Cox C, ''et al.'' |title=A polymorphism, R653Q, in the trifunctional enzyme methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase/formyltetrahydrofolate synthetase is a maternal genetic risk factor for neural tube defects: report of the Birth Defects Research Group. |journal=Am. J. Hum. Genet. |volume=71 |issue= 5 |pages= 1207-15 |year= 2003 |pmid= 12384833 |doi= }}
*{{cite journal   |vauthors=Parle-McDermott A, Mills JL, Kirke PN, etal |title=MTHFD1 R653Q polymorphism is a maternal genetic risk factor for severe abruptio placentae. |journal=Am. J. Med. Genet. A |volume=132 |issue= 4 |pages= 365–8 |year= 2005 |pmid= 15633187 |doi= 10.1002/ajmg.a.30354 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Parle-McDermott A, Pangilinan F, Mills JL, etal |title=A polymorphism in the MTHFD1 gene increases a mother's risk of having an unexplained second trimester pregnancy loss. |journal=Mol. Hum. Reprod. |volume=11 |issue= 7 |pages= 477–80 |year= 2005 |pmid= 16123074 |doi= 10.1093/molehr/gah204 }}
*{{cite journal | author=Gevaert K, Goethals M, Martens L, ''et al.'' |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566-9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
*{{cite journal  |vauthors=Kohlmeier M, da Costa KA, Fischer LM, Zeisel SH |title=Genetic variation of folate-mediated one-carbon transfer pathway predicts susceptibility to choline deficiency in humans. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=102 |issue= 44 |pages= 16025–30 |year= 2005 |pmid= 16236726 |doi= 10.1073/pnas.0504285102  | pmc=1276051 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=De Marco P, Merello E, Calevo MG, etal |title=Evaluation of a methylenetetrahydrofolate-dehydrogenase 1958G>A polymorphism for neural tube defect risk. |journal=J. Hum. Genet. |volume=51 |issue= 2 |pages= 98–103 |year= 2006 |pmid= 16315005 |doi= 10.1007/s10038-005-0329-6 }}
*{{cite journal  | author=Parle-McDermott A, Mills JL, Kirke PN, ''et al.'' |title=MTHFD1 R653Q polymorphism is a maternal genetic risk factor for severe abruptio placentae. |journal=Am. J. Med. Genet. A |volume=132 |issue= 4 |pages= 365-8 |year= 2005 |pmid= 15633187 |doi= 10.1002/ajmg.a.30354 }}
*{{cite journal  |vauthors=Sun J, Xu Y, Zhu Y, Lu H |title=Methylenetetrahydrofolate reductase gene polymorphism, homocysteine and risk of macroangiopathy in Type 2 diabetes mellitus. |journal=J. Endocrinol. Invest. |volume=29 |issue= 9 |pages= 814–20 |year= 2007 |pmid= 17114913 |doi= 10.1007/bf03347376}}
*{{cite journal | author=Parle-McDermott A, Pangilinan F, Mills JL, ''et al.'' |title=A polymorphism in the MTHFD1 gene increases a mother's risk of having an unexplained second trimester pregnancy loss. |journal=Mol. Hum. Reprod. |volume=11 |issue= 7 |pages= 477-80 |year= 2005 |pmid= 16123074 |doi= 10.1093/molehr/gah204 }}
*{{cite journal   |vauthors=Ewing RM, Chu P, Elisma F, etal |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue= 1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 | pmc=1847948 }}
*{{cite journal  | author=Kohlmeier M, da Costa KA, Fischer LM, Zeisel SH |title=Genetic variation of folate-mediated one-carbon transfer pathway predicts susceptibility to choline deficiency in humans. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=102 |issue= 44 |pages= 16025-30 |year= 2005 |pmid= 16236726 |doi= 10.1073/pnas.0504285102 }}
*{{cite journal | author=De Marco P, Merello E, Calevo MG, ''et al.'' |title=Evaluation of a methylenetetrahydrofolate-dehydrogenase 1958G>A polymorphism for neural tube defect risk. |journal=J. Hum. Genet. |volume=51 |issue= 2 |pages= 98-103 |year= 2006 |pmid= 16315005 |doi= 10.1007/s10038-005-0329-6 }}
*{{cite journal  | author=Sun J, Xu Y, Zhu Y, Lu H |title=Methylenetetrahydrofolate reductase gene polymorphism, homocysteine and risk of macroangiopathy in Type 2 diabetes mellitus. |journal=J. Endocrinol. Invest. |volume=29 |issue= 9 |pages= 814-20 |year= 2007 |pmid= 17114913 |doi=  }}
*{{cite journal  | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue= |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
}}
{{refend}}
{{refend}}


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Latest revision as of 07:01, 4 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

C-1-tetrahydrofolate synthase, cytoplasmic also known as C1-THF synthase is an enzyme that in humans is encoded by the MTHFD1 (methylenetetrahydrofolate dehydrogenase 1) gene.[1][2][3]

Function

This gene encodes a protein that possesses three distinct enzymatic activities, methylenetetrahydrofolate dehydrogenase (1.5.1.5), methenyltetrahydrofolate cyclohydrolase (3.5.4.9) and formate–tetrahydrofolate ligase (6.3.4.3). Each of these activities catalyzes one of three sequential reactions in the interconversion of 1-carbon derivatives of tetrahydrofolate, which are substrates for methionine, thymidylate, and de novo purine syntheses. The trifunctional enzymatic activities are conferred by two major domains, an aminoterminal portion containing the dehydrogenase and cyclohydrolase activities and a larger synthetase domain.[3][4]

References

  1. ↑ Hum DW, Bell AW, Rozen R, MacKenzie RE (Dec 1988). "Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase". J Biol Chem. 263 (31): 15946–50. PMID 3053686.
  2. ↑ Rozen R, Barton D, Du J, Hum DW, MacKenzie RE, Francke U (Jun 1989). "Chromosomal localization of the gene for the human trifunctional enzyme, methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase". Am J Hum Genet. 44 (6): 781–6. PMC 1715669. PMID 2786332.
  3. ↑ 3.0 3.1 "Entrez Gene: MTHFD1 methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 1, methenyltetrahydrofolate cyclohydrolase, formyltetrahydrofolate synthetase".
  4. ↑ Watkins D, Schwartzentruber JA, Ganesh J, Orange JS, Kaplan BS, Nunez LD, Majewski J, Rosenblatt DS (September 2011). "Novel inborn error of folate metabolism: identification by exome capture and sequencing of mutations in the MTHFD1 gene in a single proband". J. Med. Genet. 48 (9): 590–2. doi:10.1136/jmedgenet-2011-100286. PMID 21813566.

Further reading


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