Purification and Characterization of a Monohalomethane-producing Enzyme S-adenosyl-L-methionine: Halide Ion Methyltransferase from a Marine Microalga, Pavlova pinguis

Ohsawa, Noboru; Tsujita, Mika; Morikawa, Satoru

doi:10.1271/bbb.65.2397

Cited by 42 publications

(32 citation statements)

References 34 publications

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Section: Introductionmentioning

confidence: 99%

“…The huge preference for AdoMet over other methyl donors, such as folate, reflects favorable energetics resulting from the charged methylsulfonium center: the ΔG° for (AdoMet + Hcy → AdoHcy + Met) is −17 kcal mol −1 -over double that for (ATP → ADP + P i ) [1]. Methylation substrates range in size from arsenite to DNA and proteins, and the atomic targets can be carbon, oxygen, nitrogen, sulfur or even halides [2,3].The first structure of an AdoMet-dependent methyltransferase (MTase), determined in 1993, was for the DNA C5-cytosine MTase M.HhaI [4]. For several years thereafter, a variety of additional MTases, with a wide range of different substrates, were found to share the same basic structure.…”

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confidence: 99%

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Many paths to methyltransfer: a chronicle of convergence

Schubert

Blumenthal

Cheng

2003

Trends in Biochemical Sciences

808

873

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S-adenosyl-L-methionine (AdoMet) dependent methyltransferases (MTases) are involved in biosynthesis, signal transduction, protein repair, chromatin regulation and gene silencing. Five different structural folds (I-V) have been described that bind AdoMet and catalyze methyltransfer to diverse substrates, although the great majority of known MTases have the Class I fold. Even within a particular MTase class the amino-acid sequence similarity can be as low as 10%. Thus, the structural and catalytic requirements for methyltransfer from AdoMet appear to be remarkably flexible.'There are many paths to the top of the mountain, but the view is always the same.'…Chinese proverb [(1996) The Columbia World of Quotations, New York Columbia University Press] Following ATP, S-adenosyl-L-methionine (AdoMet) is the second most widely used enzyme substrate [1]. The majority of AdoMet-dependent reactions involve methyltransfer, leaving the product S-adenosyl-L-homocysteine (AdoHcy). The huge preference for AdoMet over other methyl donors, such as folate, reflects favorable energetics resulting from the charged methylsulfonium center: the ΔG° for (AdoMet + Hcy → AdoHcy + Met) is −17 kcal mol −1 -over double that for (ATP → ADP + P i ) [1]. Methylation substrates range in size from arsenite to DNA and proteins, and the atomic targets can be carbon, oxygen, nitrogen, sulfur or even halides [2,3].The first structure of an AdoMet-dependent methyltransferase (MTase), determined in 1993, was for the DNA C5-cytosine MTase M.HhaI [4]. For several years thereafter, a variety of additional MTases, with a wide range of different substrates, were found to share the same basic structure. More recently however, AdoMet-dependent methylation has been found to be the target of functional convergence that is catalyzed by enzymes with remarkably distinct structures. The Protein Data Bank (PDB) currently includes >100 structures for 50 distinct AdoMet-dependent MTases from 31 different classes of enzymes as defined by the Enzyme Classification (EC) system (Table 1; for a more extensive list see Ref.[5]).The purpose of this review is to compare and contrast the five known structurally distinct families of AdoMet-dependent MTases (Classes I-V). The phenomenon of enzymes from distinct structural families catalyzing the same reaction, termed enzyme analogy, has been noted for several decades [6] pluripotency that can be shaped by mutation and selection [7,8]. This can lead to a given protein structure playing several distinct catalytic roles [9], but also results in distinct protein structures playing a common catalytic role. Perhaps such flexibility is particularly easy where highly exergonic reactions are involved. As ATP is the only enzyme substrate more widely used than AdoMet, it seems logical that the current champion for greatest number of analogous families is the ATP-dependent protein phosphoryltransferases (protein kinases), with seven known structurally distinct families [10]. Nonetheless, this degree of analogy appears to be quite ra...

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Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

Many paths to methyltransfer: a chronicle of convergence

Schubert

Blumenthal

Cheng

2003

Trends in Biochemical Sciences

808

873

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“…In the tree, HOL proteins in Cluster II (Brassicales plants), Cluster III (non-Brassicales dicotyledonous plants), and Cluster IV (monocotyledonous plants) were located near each other, which implies that these HOL proteins have a common physiological role in land plants (Nagatoshi and Nakamura 2009). HOL homologous proteins were also found in algae (Ohsawa et al 2001;Toda and Itoh 2011) and fungi (Saxena et al 1998) in addition to the plant HOL proteins. OsHOL1 and OsHOL2 belong to Cluster IV, together with other HOL proteins of monocotyledonous plants.…”

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confidence: 99%

Rice OsHOL1 and OsHOL2 proteins have S-adenosyl-L-methionine-dependent methyltransferase activities toward iodide ions

Takekawa

Nakamura

2012

Plant Biotechnology

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“…Methyl group tran sfer is an alkylation reaction, and the atomic targets for the reaction can be carbon, oxygen, nitrogen, sulfur or even halides (1)(2)(3).…”

Section: Introductionmentioning

confidence: 99%

rRNA Methyltransferases and their Role in Resistance to Antibiotics

Morić¹,

Savic²,

Ilić-Tomič³

et al. 2010

Journal of Medical Biochemistry

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MTaze metiluju nukleinske kiseline (DNK, RNK) i proteine, moduli{u}i tako njihovu aktivnost, funkciju i strukturnu organizaciju. Metilacija G1405 ili A1408 baza u 16S rRNK mikroorganizama koji proizvode aminoglikozide obezbe |u -je rezistenciju na sopstvene toksi~ne pro izvode. Ovaj mehanizam rezistencije je donedavno bio opi san samo kod proizvo|a~a antibiotika. Od 2003. godine i kod patogenih bakterija bele`i se neprestan porast rezi sten cije na aminoglikozide putem ovog mehanizma, {to predstavlja veliku pretnju efikasnoj upotrebi aminoglikozida u klini~koj praksi. Jedno od mogu}ih re{enja problema le`i u razvoju novih jedinjenja koja bi efikasno delovala na nova mesta u okviru ribozoma. Drugi pristup re{avanju ovog problema uklju~uje razvoj inhibitora MTaza odgovornih za rezisten ciju, sa idejom da se onemogu}i modifikacija bakte rijske rRNK i na taj na~in vrati terapeutska efikasnost postoje}im aminogliko zidima. Fundamentalna istra`ivanja vezana za proteinsku ekspresiju, potpuno razumevanje mehanizma rezistencije kao i razre{enje tercijarne strukture proteina su neophodan preduslov za primenu inhibitora 16S rRNK MTaza u medicini.

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Purification and Characterization of a Monohalomethane-producing Enzyme S-adenosyl-L-methionine: Halide Ion Methyltransferase from a Marine Microalga, Pavlova pinguis

Cited by 42 publications

References 34 publications

Many paths to methyltransfer: a chronicle of convergence

Many paths to methyltransfer: a chronicle of convergence

Rice OsHOL1 and OsHOL2 proteins have S-adenosyl-L-methionine-dependent methyltransferase activities toward iodide ions

rRNA Methyltransferases and their Role in Resistance to Antibiotics

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