グルタミン酸ホルムイミドイルトランスフェラーゼ
WordNet
- a salt or ester of glutamic acid
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/09/07 14:53:59」(JST)
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| Formiminotransferase domain, N-terminal subdomain |
|
the crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase.
|
| Identifiers |
| Symbol |
FTCD_N |
| Pfam |
PF07837 |
| InterPro |
IPR012886 |
| SCOP |
1qd1 |
| SUPERFAMILY |
1qd1 |
| Available protein structures: |
| Pfam |
structures |
| PDB |
RCSB PDB; PDBe; PDBj |
| PDBsum |
structure summary |
|
| Formiminotransferase domain |
|
the crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase.
|
| Identifiers |
| Symbol |
FTCD |
| Pfam |
PF02971 |
| InterPro |
IPR013802 |
| SCOP |
1qd1 |
| SUPERFAMILY |
1qd1 |
| Available protein structures: |
| Pfam |
structures |
| PDB |
RCSB PDB; PDBe; PDBj |
| PDBsum |
structure summary |
|
In molecular biology, Glutamate formimidoyltransferase is a methyltransferase enzyme which uses tetrahydrofolate as part of histidine catabolism. It catalyses two reactions:
- 5-formimidoyltetrahydrofolate + L-glutamate <=> tetrahydrofolate + N-formimidoyl-L-glutamate
- 5-formyltetrahydrofolate + L-glutamate <=> tetrahydrofolate + N-formyl-L-glutamate
It is classified under EC 2.1.2.5 and in mammals is found as part of a bifunctional enzyme that also has formimidoyltetrahydrofolate cyclodeaminase activity.[1]
Structure
The formiminotransferase (FT) domain of formiminotransferase-cyclodeaminase (FTCD) forms a homodimer, with each protomer comprising two subdomains. The formiminotransferase domain has an N-terminal subdomain that is made up of a six-stranded mixed beta-pleated sheet and five alpha helices, which are arranged on the external surface of the beta sheet. This, in turn, faces the beta-sheet of the C-terminal subdomain to form a double beta-sheet layer. The two subdomains are separated by a short linker sequence, which is not thought to be any more flexible than the remainder of the molecule. The substrate is predicted to form a number of contacts with residues found in both the N-terminal and C-terminal subdomains.[2] In humans, deficiency of this enzyme results in a disease phenotype.[3]
References
- ^ MacKenzie RE, Aldridge M, Paquin J (10 October 1980). "The bifunctional enzyme formiminotransferase-cyclodeaminase is a tetramer of dimers". J. Biol. Chem. 255 (19): 9474–8. PMID 7410436.
- ^ Kohls D, Sulea T, Purisima EO, MacKenzie RE, Vrielink A (January 2000). "The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme". Structure. 8 (1): 35–46. doi:10.1016/S0969-2126(00)00078-2. PMID 10673422.
- ^ Hilton JF, Christensen KE, Watkins D, Raby BA, Renaud Y, de la Luna S, Estivill X, MacKenzie RE, Hudson TJ, Rosenblatt DS (July 2003). "The molecular basis of glutamate formiminotransferase deficiency". Hum. Mutat. 22 (1): 67–73. doi:10.1002/humu.10236. PMID 12815595.
External links
- Glutamate formimidoyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
|
Transferase: one carbon transferases (EC 2.1)
|
|
| 2.1.1: Methyl- |
| N- |
- Histamine N-methyltransferase
- Phenylethanolamine N-methyltransferase
- Amine N-methyltransferase
- Phosphatidylethanolamine N-methyltransferase
|
|
| O- |
- 5-hydroxyindole-O-methyltransferase/Acetylserotonin O-methyltransferase
- Catechol-O-methyl transferase
|
|
| Homocysteine |
- Betaine-homocysteine methyltransferase
- Homocysteine methyltransferase
- Methionine synthase
|
|
| Other |
- Phosphatidyl ethanolamine methyltransferase
- DNMT3B
- Histone methyltransferase
- Thymidylate synthase
- DNA methyltransferase
- Thiopurine methyltransferase
|
|
|
2.1.2: Hydroxymethyl-,
Formyl- and Related |
| Hydroxymethyltransferase |
- Serine hydroxymethyltransferase
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
|
|
| Formyltransferase |
- Phosphoribosylglycinamide formyltransferase
- Inosine monophosphate synthase
|
|
| Other |
- Glutamate formimidoyltransferase
- Aminomethyltransferase
|
|
|
2.1.3: Carboxy-
and Carbamoyl |
| Carboxy |
- methylmalonyl-CoA carboxytransferase
|
|
| Carbamoyl |
- Aspartate carbamoyltransferase
- Ornithine carbamoyltransferase
- Oxamate carbamoyltransferase
- Putrescine carbamoyltransferase
- 3-hydroxymethylcephem carbamoyltransferase
- Lysine carbamoyltransferase
- N-acetylornithine carbamoyltransferase
|
|
|
| 2.1.4: Amidine |
- Arginine:glycine amidinotransferase
|
|
Enzymes
|
|
| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
|
|
| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
|
|
| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
|
|
| Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
|
This article incorporates text from the public domain Pfam and InterPro IPR013802
This article incorporates text from the public domain Pfam and InterPro IPR012886
UpToDate Contents
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English Journal
- Different sites of xenoantigen delivery lead to a virally induced late-onset hepatitis in mice through molecular mimicry.
- Piché C, Béland K, Lapierre P, Massie B, Alvarez F.SourceDivision of Gastroenterology, Hepatology, Nutrition, CHU Sainte-Justine, Montréal, QC, Canada.
- Liver international : official journal of the International Association for the Study of the Liver.Liver Int.2011 Oct;31(9):1306-14. doi: 10.1111/j.1478-3231.2011.02600.x. Epub 2011 Aug 4.
- BACKGROUND: Epidemiological and laboratory evidences led to the hypothesis that molecular mimicry between viruses and self-proteins could be linked to the onset of autoimmune hepatitis (AIH). Hepatotropic viruses could be good candidates, as a pro-inflammatory environment may facilitate the developm
- PMID 22093453
- Moonlighting glutamate formiminotransferases can functionally replace 5-formyltetrahydrofolate cycloligase.
- Jeanguenin L, Lara-Núñez A, Pribat A, Mageroy MH, Gregory JF 3rd, Rice KC, de Crécy-Lagard V, Hanson AD.SourceDepartment of Horticultural Sciences, University of Florida, Gainesville, Florida 32611, USA.
- The Journal of biological chemistry.J Biol Chem.2010 Dec 31;285(53):41557-66. doi: 10.1074/jbc.M110.190504. Epub 2010 Oct 15.
- 5-Formyltetrahydrofolate (5-CHO-THF) is formed by a side reaction of serine hydroxymethyltransferase. Unlike other folates, it is not a one-carbon donor but a potent inhibitor of folate enzymes and must therefore be metabolized. Only 5-CHO-THF cycloligase (5-FCL) is generally considered to do this.
- PMID 20952389
- Normal mode refinement of anisotropic thermal parameters for a supramolecular complex at 3.42-A crystallographic resolution.
- Poon BK, Chen X, Lu M, Vyas NK, Quiocho FA, Wang Q, Ma J.SourceDepartment of Bioengineering, Rice University, Houston, TX 77005, USA.
- Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2007 May 8;104(19):7869-74. Epub 2007 Apr 30.
- Here we report a normal-mode-based protocol for modeling anisotropic thermal motions of proteins in x-ray crystallographic refinement. The foundation for this protocol is a recently developed elastic normal mode analysis that produces much more accurate eigenvectors without the tip effect. The effec
- PMID 17470791
Related Links
- glu·ta·mate for·mim·i·no·trans·fer·ase an enzyme that catalyzes the transfer of the formimino moiety of N-formimino-l-glutamate to tetrahydrofolate; a deficiency of this enzyme will lead to elevated formiminoglutamate levels. glutamate ...
- Definition of glutamate formimidoyltransferase in the Definitions.net dictionary. Meaning of glutamate formimidoyltransferase. What does glutamate formimidoyltransferase mean? Information and translations of glutamate ...
★リンクテーブル★
[★]
- 英
- glutamate formimidoyltransferase
[★]
グルタミン酸、グルタメート、グルタメイト、(化合物)グルタミン酸塩