Search results for ME2

Showing 25 results out of 185

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Protein (6 results from a total of 86)

ME2

Identifier: R-HSA-9012080
Species: Homo sapiens
Compartment: mitochondrial matrix
Primary external reference: UniProt: ME2: P23368
Identifier: R-HSA-192213
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: SNRPB: P14678
Identifier: R-HSA-8865931
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: SNRPN: P63162
Identifier: R-HSA-6805759
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: P04637
Identifier: R-HSA-6804378
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: P04637
Identifier: R-HSA-8936570
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: H3C15: Q71DI3

Complex (6 results from a total of 47)

Identifier: R-HSA-9012271
Species: Homo sapiens
Compartment: mitochondrial matrix
Identifier: R-HSA-9012264
Species: Homo sapiens
Compartment: mitochondrial matrix
Identifier: R-HSA-9012259
Species: Homo sapiens
Compartment: mitochondrial matrix
Identifier: R-HSA-6805762
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-3222245
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-3222249
Species: Homo sapiens
Compartment: nucleoplasm

Set (6 results from a total of 31)

Identifier: R-HSA-8865952
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5244740
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5244522
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5638169
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5649783
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5634724
Species: Homo sapiens
Compartment: nucleoplasm

Reaction (6 results from a total of 20)

Identifier: R-HSA-9012268
Species: Homo sapiens
Compartment: mitochondrial matrix
One hallmark of cancer is altered cellular metabolism. Malic enzymes (MEs) are a family of homotetrameric enzymes that catalyse the reversible oxidative decarboxylation of L-malate to pyruvate, with a simultaneous reduction of NAD(P)+ to NAD(P)H. As MEs generate NADPH and NADH, they may play dual roles in energy production and reductive biosynthesis. Humans possess three ME isoforms; ME1 is cytosolic and utilises NADP+, ME3 is mitochondrial and can utilise NADP+ and ME2 is mitochondrial and can utililse either NAD+ or NADP+ (Chang & Tong 2003).

Mitochondrial NAD-dependent malic enzyme (ME2, aka m-NAD(P)-ME) oxidatively decarboxylates (s)-malate (MAL) to pyruvate (PYR) and CO2 using NAD+ (or NADP+) as cofactor (Loeber et al. 1991, Tao et al. 2003). ME2 exists as a dimer of dimers and requires a divalent metal such as Mg2+ for catalysis (Chang & Tong 2003, Murugan & Hung 2012). Unlike the other MEs, ME2's enzymatic activity can be allosterically activated by fumarate (FUMA) and inhibited by ATP (Yang et al. 2002). ME2 could play a critical role in cutaneous melanoma progression, the most life-threatening neoplasm of the skin. Targeting ME2 could be a novel approach to inhibiting melanoma cell proliferation and growth (Chang et al. 2015). ME2 has also been demonstrated to be involved in glioblastoma multiforme (GBM) growth, invasion and migration. Inhibition of ME2 could potentially be therapeutic in the treatment of GBM (Cheng et al. 2016).
Identifier: R-HSA-2408554
Species: Homo sapiens
Compartment: cytosol
Indolethylamine N-methyltransferase (INMT) is involved in the methylation of dimethyl selenide (Me2Se) into trimethylselenonium (Me3Se+) in tandem with S-adenosylmethionine (AdoMet) transforming into S-adenosylhomocysteine (AdoHcy). This reaction is inferred from the event in mouse (Mozier et al. 1988).
Identifier: R-HSA-4754181
Species: Homo sapiens
Compartment: nucleoplasm
All characterized lysine demethylases other than KDM1A belong to the jumonjiC domain (JmjC) containing family.The JmjC KDMs are members of the Cupin superfamily of mononuclear Fe (II) dependent oxygenases, which are characterized by the presence of a double-stranded beta-helix core fold. The JmjC KDMs require 2 oxoglutarate (2 OG) and molecular oxygen as co substrates, producing, along with formaldehyde, succinate and carbon dioxide. This hydroxylation based mechanism does not require a protonatable lysine epsilon-amine group and consequently JmjC containing demethylases are able to demethylate tri , di and monomethylated lysines. KDM5A-D (JARID1A-D) catalyse the demethylation of di- or tri-methylated lysine-5 of histone H3 (H3K4Me2/3) (Christensen et al. 2007, Klose et al. 2007, Lee et al. 2007, Secombe et al. 2007, Seward et al. 2007, Iwase et al. 2007).
Identifier: R-HSA-5661125
Species: Homo sapiens
Compartment: nucleoplasm
JMJD6 catalyses demethylation of mono- or di-methylated arginine-3 of histone H3 (H3R2Me1/2) and arginine-4 of histone H4 (H4R3Me1/2) (Chang et al. 2007). Non-histone substrates of JMJD6 arginine demethylation have also been reported (Poulard et al. 2014, Lawrence et al. 2014). Subsequent to its characterization as an arginine demethylase, JMJD6 was reported to be a lysine hydroxylase (Webby et al 2009).
Identifier: R-HSA-5661122
Species: Homo sapiens
Compartment: nucleoplasm
JMJD6 catalyses demethylation of mono- or di-methylated arginine-3 of histone H3 (H3R2Me1/2) and arginine-4 of histone H4 (H4R3Me1/2) (Chang et al. 2007). Non-histone substrates of JMJD6 arginine demethylation have also been reported (Poulard et al. 2014, Lawrence et al. 2014). Subsequent to its characterization as an arginine demethylase, JMJD6 was reported to be a lysine hydroxylase (Webby et al 2009).
Identifier: R-HSA-5212679
Species: Homo sapiens
Compartment: nucleoplasm
H4R3me2s is a direct binding target for the DNA methyltransferase DNMT3A, which interacts through the ADD domain containing the PHD motif. Loss of the H4R3me2s mark through short hairpin RNA–mediated knockdown of PRMT5 leads to reduced DNMT3A binding, loss of DNA methylation and gene activation (Zhao et al. 2009).

Chemical Compound (1 results from a total of 1)

Identifier: R-ALL-5357673
Compartment: cytosol
Primary external reference: ChEBI: dimethylselenide: 4610
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