Methyltransferase, protein

Protein phosphatase 2C Protein arginine methyltransferase Protein arginine methyltransferase Arylalkylamine N-acetyltransferase SARS Cov 3C-like protease AHAS... 

Highly populated protein domain families of H. pylori include (1) the cellular component Helicobacter outer membrane protein family (2) the sell family, which is associated with P-lactamase activity (3) members of the CagA and VacA protein families, which are secreted into host cells and are involved in pathogenesis (4) the ABC transporter family, which is associated with ATP-dependent transport of molecules across the membrane (5) the DNA methyltransferase protein domain family (6) the radical SAM (S-adenosylmethionine) family associated with various metabolic functions of pathogens and (7) the response regulator receiver domain family, which is involved in receiving the signal from the sensor domain in bacterial two-component systems. 

Protein O-methyltransferase. Protein methylase II, which methylates the y or carboxyl group of glutamic and/or aspartic acid residues has been purified from calf thymus (193) and rat and human blood (213). The recommended trivial name of this enzyme is protein O-methyltransferase (S-adenosyl-L-methionine protein O-methyltransferase EC 2.1.1.24). The enzyme catalyzes the reaction ... 

In Abramowicz DA (ed). Biocatalysis. Van Nostrand Reinhold, New York, pp 277-318 Nasser W, Chalet F, Robert-Baudouy J (1990) Purification and characterization of extracellular pectate lyase from Bacillus subtilis. Biochimie 72(9) 689-695 Neidleman SL (1991) Historical perspective on the industrial uses of biocattilysts. In Dordick JS (ed). Biocatalysts for industry. Plenum Press, New York, pp 21-33 Neuhaus W, Novalin S, Klimacek, M et al. (2006) Optimization of an innovative hoUow-fiber process to produce lactose-reduced skim milk. Appl Biochem Biotechnol 134(1) 1-14 Nield BS, Willows RD, Torda AE et al. (2002) New enzymes from environmental cassette arrays functional attributes of a phosphotransferase and an RNA-methyltransferase. Protein Sci 13 1651-1659... 

Gene Methylators-Demethylators Acetylators-Deacetylators. Early discovered histone lysine (K) methyltransferase protein domains are those from Paramecium... 

The farnesylation and subsequent processing of the Ras protein. Following farnesylation by the FTase, the carboxy-terminal VLS peptide is removed by a prenyl protein-specific endoprotease (PPSEP) in the ER, and then a prenylprotein-specific methyltransferase (PPSMT) donates a methyl group from S-adenosylmethionine (SAM) to the carboxy-terminal S-farnesylated cysteine. Einally, palmitates are added to cysteine residues near the C-terminus of the protein. 

Barton and coworkers have shown that proteins can in fact modulate the DNA electron transfer [168]. Methyltransferases are enzymes that recognize distinct DNA sequences, e.g., 5 -G CGC-3, and effect methylation by extrading the target base cytosine ( C) completely out of the DNA duplex while the remainder of the double helix is left intact. The methyltransferase Hha 1-DNA complex is a well-characterized example, revealing that the structure of the DNA is significantly but locally distorted [169,170]. In a recent study, Raj ski et al. used DNA duplex 20 containing the M.Hha I binding site between two oxidizable 5 -GG-3 sites [168] (Fig. 20). The duplex contains a complementary strand, selectively 5 -modified with a Rh intercalator that can function as a photooxidant. Upon... 

FIG. 20 DNA duplex 20 used for studies regarding the protein-modulated DNA electron transfer. Methyltransferase M.Hhal is capable of binding to the shadowed recognition site between two oxidizable 5 -GG-3 sites (outlined letters). The complementary strand of the duplex contains the Rh intercalator, [Rh(phi)2bpy ], at its 5 end, which can function as a photooxidant. (Adapted from Ref. 168.)... 

In these experiments the pectin methyltransferase activity in vitro was generally only a few picokatal g" of protein, due mainly to the limited amount of SAM and endogeneous polysaccharide substrate. 

Murray, Jr., E. D. and Clarke, S., Synthetic peptide substrates for the erythrocyte protein carboxyl methyltransferase, J. Biol. Chem., 259, 10722, 1984. 

A common way to benefit from the ability to combine different molecular orbital methods in ONIOM is to combine a DFT or ab-initio description of the reactive region with a semi-empirical treatment of the immediate protein environment, including up to 1000 atoms. Due to the requirement for reliable semi-empirical parameters, as discussed in Section 2.2.1, this approach has primarily been used for non-metal or Zn-enzymes. Examples include human stromelysin-1 [83], carboxypeptidase [84], ribonucleotide reductase (substrate reaction) [85], farnesyl transferase [86] and cytosine deaminase [87], Combining two ab-initio methods of different accuracy is not common in biocatalysis applications, and one example from is an ONIOM (MP2 HF) study of catechol O-methyltransferase [88],... 

Yeates TO (2002) Structures of set domain proteins protein lysine methyltransferases make their mark. Cell 111 5-7... 

Trievel RC, Beach BM, Dirk LMA, Houtz RL, Hurley JH (2002) Structure and catalytic mechanism of a set domain protein methyltransferase. Cell 111 91—103... 

Fig. 13 DNA-protein CT reactions. The DNA-bound protein, methyltransferase Hhal (mutant Q237W), flips a base out of the DNA double helix and inserts a trytophan side chain leaving the /r-stack largely unperturbed. This intercalated trytophan moiety transfers an electron to [Ru(bpy )(dppz)(phen)]3+, generated by flash quench, over 50 A away. Adapted from [164]... 

Figure 1 Covalent modifications of DNA and histones play a fundamental role in the regulation of differentiation and development. The writers, readers, and erasers of this dynamic code are potentially amenable to modulation with small molecules. Lysine methylation is a critical posttranslational modification influencing chromatin function (PMT = protein lysine methyltransferase, royal family proteins bind KMe, KDM = lysine demethylase).

Figure 2 Selected human protein lysine methyltransferases and their target sites on histones [11].

L, loading module DH, dehydratase KS, p-ketosynthase KR, ketoreductase MT methyltransferase PS, pyran synthase DHh and KRh are DH and KR-like sequences, together with the FkbH domain, they are involved in the formation of D-lactate starter unit HMG-CS, hydroxy-methyl-glutaryl CoA synthase. Acyl-carrier-protein domains are shown as small filled balls with chain attached by the thiol group. The box shows the HMG-CS pathway for the formation of exocyclic enoate. 

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