gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Adenosylhomocysteinase at 13

AdoHcyase, S-adenosyl-L-homocysteine hydrolase, Adenosylhomocysteinase
Top mentioned proteins: ACID, Ado, AdoMet, HAD, CAN
Papers on AdoHcyase
An enzyme captured in two conformational states: crystal structure of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii.
Jaskolski et al., Poznań, Poland. In Acta Crystallogr D Biol Crystallogr, Jan 2016
S-Adenosyl-L-homocysteine hydrolase (SAHase) is involved in the enzymatic regulation of S-adenosyl-L-methionine (SAM)-dependent methylation reactions.
Instar-dependent systemic RNA interference response in Leptinotarsa decemlineata larvae.
Li et al., Nanjing, China. In Pestic Biochem Physiol, Sep 2015
In this study, RNAi efficiency by double-stranded RNA (dsRNA) targeting S-adenosyl-L-homocysteine hydrolase (LdSAHase) was compared among L. decemlineata first- to fourth-instar larvae.
Discovery and structural analyses of S-adenosyl-L-homocysteine hydrolase inhibitors based on non-adenosine analogs.
Sunada et al., Yokohama, Japan. In Bioorg Med Chem, Sep 2015
Optimization of a new series of S-adenosyl-L-homocysteine hydrolase (AdoHcyase) inhibitors based on non-adenosine analogs led to very potent compounds 14n, 18a, and 18b with IC50 values of 13 ± 3, 5.0 ± 2.0, and 8.5 ± 3.1 nM, respectively.
S-Inosyl-L-Homocysteine Hydrolase, a Novel Enzyme Involved in S-Adenosyl-L-Methionine Recycling.
White et al., Blacksburg, United States. In J Bacteriol, Jul 2015
Here, we show that the annotated S-adenosyl-L-homocysteine hydrolase in Methanocaldococcus jannaschii is specific for the hydrolysis and synthesis of S-inosyl-L-homocysteine, not S-adenosyl-L-homocysteine.
Structural insights into the reaction mechanism of S-adenosyl-L-homocysteine hydrolase.
Tanaka et al., Tokyo, Japan. In Sci Rep, 2014
S-adenosyl-L-homocysteine hydrolase (SAH hydrolase or SAHH) is a highly conserved enzyme that catalyses the reversible hydrolysis of SAH to L-homocysteine (HCY) and adenosine (ADO).
Discovery of S-adenosyl-L-homocysteine hydrolase inhibitors based on non-adenosine analogs.
Setsuta et al., Toda, Japan. In Bioorg Med Chem Lett, 2014
High throughput screening using Automated Ligand Identification System (ALIS) resulted in the discovery of a new series of S-adenosyl-L-homocysteine hydrolase inhibitors based on non-adenosine analogs.
Highly enhanced electrochemiluminescent strategy for tumor biomarkers detection with in situ generation of L-homocysteine for signal amplification.
Bai et al., Chongqing, China. In Anal Chim Acta, 2014
In the reaction of biological methylation, S-adenosyl-L-homocysteine hydrolase (SAHH) catalyzed the reversible hydrolysis of S-adenosyl-L-homocysteine (SAH) to produce L-Hcys, which was inducted into ECL system to construct the immunosensor for signal amplification in this work.
Deazaneplanocin a is a promising drug to kill multiple myeloma cells in their niche.
Sola et al., Caen, France. In Plos One, 2013
Deazaneplanocin A (DZNep), a S-adenosyl-L-homocysteine hydrolase inhibitor, targets enhancer of zest homolog 2 (EZH2), a component of polycomb repressive complex 2 (PRC2) and is capable to induce the death of cancer cells.
Allelic variation within the S-adenosyl-L-homocysteine hydrolase gene family is associated with wood properties in Chinese white poplar (Populus tomentosa).
Zhang et al., In Bmc Genet, 2013
BACKGROUND: S-adenosyl-l-homocysteine hydrolase (SAHH) is the only eukaryotic enzyme capable of S-adenosyl-l-homocysteine (SAH) catabolism for the maintenance of cellular transmethylation potential.
[Blue-light induced expression of S-adenosy-L-homocysteine hydrolase-like gene in Mucor amphibiorum RCS1].
Zhong et al., Nanchang, China. In Wei Sheng Wu Xue Bao, 2013
OBJECTIVE: To determine blue-light induced expression of S-adenosyl-L-homocysteine hydrolase-like (sahhl) gene in fungus Mucor amphibiorum RCS1.
S-adenosyl-L-homocysteine hydrolase and methylation disorders: yeast as a model system.
Keller et al., Graz, Austria. In Biochim Biophys Acta, 2013
S-adenosyl-L-homocysteine hydrolase is the only eukaryotic enzyme capable of reversible AdoHcy hydrolysis to adenosine and homocysteine and, thus, relief from AdoHcy inhibition.
[Structural biology for developing antimalarial compounds].
Nakamura et al., In Yakugaku Zasshi, 2012
One example is the structural studies for S-adenosyl-L-homocysteine hydrolase from Plasmodium falciparum (PfSAHH) and the other example is those for 1-deoxy-D-xylulose reductoisomerase from Plasmodium falciparum (PfDXR).
[S-adenosyl-L-homocysteine hydrolase as an attractive target for antimicrobial drugs].
Nakanishi, Gifu, Japan. In Yakugaku Zasshi, 2007
S-Adenosyl-L-homocysteine (SAH) hydrolase catalyzes breakdown of SAH, which arises after S-adenosylmethionine-dependent methylation, into adenosine and homocysteine.
S-Adenosylhomocysteine hydrolase as a target for intracellular adenosine action.
Osswald et al., Tübingen, Germany. In Trends Pharmacol Sci, 2004
S-Adenosylhomocysteine hydrolase (AdoHcyase) controls intracellular levels of S-adenosylhomocysteine (AdoHcy).
Targeting "hydrolytic" activity of the S-adenosyl-L-homocysteine hydrolase.
Wnuk, Miami, United States. In Mini Rev Med Chem, 2001
Substrates that are specific for the "hydrolytic" activities of AdoHcy hydrolase have been recently identified.
share on facebooktweetadd +1mail to friends