MTRR
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Official Full Name
5-methyltetrahydrofolate-homocysteine methyltransferase reductase
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Overview
Methionine is an essential amino acid required for protein synthesis and one-carbon metabolism. Its synthesis is catalyzed by the enzyme methionine synthase. Methionine synthase eventually becomes inactive due to the oxidation of its cob(I)alamin cofactor. The protein encoded by this gene regenerates a functional methionine synthase via reductive methylation. It is a member of the ferredoxin-NADP(+) reductase (FNR) family of electron transferases. Patients of the cbl-E complementation group of disorders of folate/cobalamin metabolism are defective in reductive activation of methionine synthase. Alternative splicing of this gene results in multiple transcript variants encoding distinct isoforms. -
Synonyms
MTRR; 5-methyltetrahydrofolate-homocysteine methyltransferase reductase; methionine synthase reductase; cblE; [methionine synthase] cobalamin methyltransferase (cob(II)alamin reducing); 5 methyltetrahydrofolate homocysteine methyltransferase reductase; Methionine synthase reductase, mitochondrial; MGC129643; MSR; OTTHUMP00000115546; OTTHUMP00000220821; [methionine synthase]-cobalamin methyltransferase (cob(II)alamin reducing);
- Cell & Tissue Lysates
- Recombinant Proteins
- Protein Pre-coupled Magnetic Beads
- Human
- Mouse
- Rat
- E.coli
- HEK293
- Mammalian Cell
- Wheat Germ
- Yeast
- GST
- His
- His (Fc)
- Avi
- N/A
- N
- Involved Pathway
- Protein Function
- Interacting Protein
MTRR involved in several pathways and played different roles in them. We selected most pathways MTRR participated on our site, such as Biological oxidations, Cobalamin (Cbl, vitamin B12) transport and metabolism, Defective MTR causes methylmalonic aciduria and homocystinuria type cblG, which may be useful for your reference. Also, other proteins which involved in the same pathway with MTRR were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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Biological oxidations | SULT1ST5;CYP2K22;CYP2Y3;PRKRA;CYP3C1;UGT1B1;Sult2a2;SULT1C2;CYP2C9 |
Cobalamin (Cbl, vitamin B12) transport and metabolism | CTRC;MTRR;CD320;AMN;ELA2;MMADHC;LOC100686744;CTRB1;CBLC-1 |
Defective MTR causes methylmalonic aciduria and homocystinuria type cblG | |
Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE | |
Defects in cobalamin (B12) metabolism | MMAA;AMN;MTRR;MMADHC |
Defects in vitamin and cofactor metabolism | MMADHC;MTRR;MMAA;AMN |
Disease | CHMP4C;JAG1;AP2B1;OPN1LW;GPC5;CTBP2;TLR10;HEY2;EPM2A |
Diseases of metabolism | SFTPC;CYP11A1;MMAA;AMN;CCDC59;GYG1;FDXR;MMADHC;FDX1 |
MTRR has several biochemical functions, for example, FAD binding, FMN binding, NADP binding. Some of the functions are cooperated with other proteins, some of the functions could acted by MTRR itself. We selected most functions MTRR had, and list some proteins which have the same functions with MTRR. You can find most of the proteins on our site.
Function | Related Protein |
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FAD binding | CYB5R3;COQ6;DAO;DAO1;DDO;MICAL2B;AGPS;MTRR;PRODH |
FMN binding | NOS1;NOS3;NOS2;MTRR;HAO2;TYW1;CREG1;NOS2B;HAO1 |
NADP binding | MTHFR;NOX1;NOX5;H6PD;CAT;DPYD;FMO5;MIOX;MTRR |
NADPH binding | DHFR;CRYZ;MTRR;KCNAB1;GRHPR;FASN;DECR1;CBR3;QDPR |
NADPH-hemoprotein reductase activity | POR;NOS2A;CYP2J6;NDOR1;NOS2B;MTRR;NOS2;NOS3;NOS1 |
[methionine synthase] reductase activity | |
aquacobalamin reductase (NADPH) activity | |
flavin adenine dinucleotide binding | CHDH;NOS3;PPOX;FMO1;FOXRED2;TXNRD2;MTHFR;ACADL;CYBB |
iron ion binding | CH25HL2;CYP2D26;CYP46A1.1;HBG2;CYP2C19;TPH1;CYP2X7;ALOX12;CYP4F11 |
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen | COQ6;CYP4F11;CYP11A1;CYP11B2;CYP4F18;NDOR1;MTRR;MICAL1;POR |
oxidoreductase activity, oxidizing metal ions, NAD or NADP as acceptor | |
protein binding | MESDC1;MTRR;RPS18;LGI4;RTN4R;ZYX;LYRM2;USP1;LGALS2 |
MTRR has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with MTRR here. Most of them are supplied by our site. Hope this information will be useful for your research of MTRR.
FLJ13057
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