Results 271 to 280 of about 574,974 (306)

Universal Catalytic Domain Structure of AdoMet-dependent Methyltransferases

Journal of Molecular Biology, 1995
The DNA methyltransferases, M.HhaI and M.TaqI, and catechol O-methyl-transferase (COMT) catalyze the transfer of a methyl group from the cofactor S-adenosyl-L-methionine (AdoMet) to carbon-5 of cytosine, to nitrogen-6 of adenine, and to a hydroxyl group of catechol, respectively. The catalytic domains of the bilobal proteins, M.HhaI and M.TaqI, and the
G, Schluckebier, M, O'Gara, W, Saenger, X, Cheng   +3 more
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Catalytic and Regulatory Domains of Doublecortin Kinase-1

Biochemistry, 2003
Doublecortin kinase-1 (DCK1) is a newly described multidomain protein kinase with a sequence significantly similar to those of both CaM kinases (CaMKs) and doublecortin, the product of the gene mutated in X-linked lissencephaly/double cortex syndrome, a severe developmental disorder of the nervous system.
Limin, Shang, Young-Guen, Kwon, Sandip, Nandy, David S, Lawrence, Arthur M, Edelman   +4 more
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Yeast adenylate cyclase catalytic domain is carboxy terminal

Current Genetics, 1986
Subcloning of DNA fragments from the gene coding for yeast adenylate cyclase has permitted, after complementation studies in S. cerevisiae cdc35 mutants as well as E. coli cya mutants, to identify the sequence coding for the catalytic domain of the protein.
P, Masson, G, Lenzen, J M, Jacquemin, A, Danchin   +3 more
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Thioether Macrocyclic Peptides Selected against TET1 Compact Catalytic Domain Inhibit TET1 Catalytic Activity

ChemBioChem, 2018
AbstractThe ten–eleven translocation (TET) protein family, consisting of three isoforms (TET1/2/3), have been found in mammalian cells and have a crucial role in 5‐methylcytosine demethylation in genomic DNA through the catalysis of oxidation reactions assisted by 2‐oxoglutarate (2OG). DNA methylation/demethylation contributes to the regulation of gene
Kosuke Nishio, Roman Belle, Takayuki Katoh, Akane Kawamura, Toru Sengoku, Kazuharu Hanada, Noboru Ohsawa, Mikako Shirouzu, Shigeyuki Yokoyama, Hiroaki Suga   +9 more
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Inhibitors of the catalytic domain of mitochondrial ATP synthase

Biochemical Society Transactions, 2006
An understanding of the mechanism of ATP synthase requires an explanation of how inhibitors act. The catalytic F1-ATPase domain of the enzyme has been studied extensively by X-ray crystallography in a variety of inhibited states. Four independent inhibitory sites have been identified by high-resolution structural studies.
J R, Gledhill, J E, Walker
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Structural analysis of the catalytic domain of tetanus neurotoxin

Toxicon, 2005
Clostridium neurotoxins, comprising the tetanus neurotoxin and the seven antigenically distinct botulinum neurotoxins (BoNT/A-G), are among the known most potent bacterial protein toxins to humans. Although they have similar function, sequences and three-dimensional structures, the substrate specificity and the selectivity of peptide bond cleavage are ...
Krishnamurthy N, Rao, Desigan, Kumaran, Thomas, Binz, Subramanyam, Swaminathan   +3 more
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Structure of the Isolated Catalytic Domain of Diphtheria Toxin

Biochemistry, 1995
The structure of the isolated catalytic domain of diphtheria toxin at pH 5.0 was determined by X-ray crystallography at 2.5 A resolution and refined to an R-factor of 19.7%. The domain is bound to its endogenous inhibitor adenylyl(3'-->5')uridine 3'-monophosphate (ApUp). The structure of this 190-residue domain, which was expressed in and isolated from
M S, Weiss, S R, Blanke, R J, Collier, D, Eisenberg   +3 more
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Catalytic diversity of cupin domain-containing enzymes

2018
<p>Cupins are a large superfamily of enzymatic and non-enzymatic members that contain a conserved β-barrel domain, or double-stranded β-helix (DSBH) fold. The cupin superfamily is one of the most functionally diverse groups of proteins known to exist.
Nicholas Jay Schnicker, Mishtu Dey, Amnon Kohen, Daniel M. Quinn, James B. Gloer, Ernesto J. Fuentes   +5 more
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Polyamines and the catalytic domain of protein kinase C

Life Sciences, 1988
The effect of polyamines on the catalytic domain of protein kinase C from rat brain was investigated. It was found that the addition of spermine strongly inhibited phosphorylation activity toward histone H1 as substrate. This tetramine, at millimolar concentrations, was most potently effective while triamines and diamines were almost uneffective ...
G, Mezzetti, M G, Monti, M S, Moruzzi
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Pin1 Catalytic and WW Domain Ligands

2014
Ph. D.
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