Purification, characterization, and molecular cloning of S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase from Methanobacterium ivanovii

Blanche, Francis; Robin, Charles; Couder, M; Faucher, Didier; Cauchois, L; Cameron, Béatrice; Crouzet, J

doi:10.1128/jb.173.15.4637-4645.1991

Cited by 48 publications

(24 citation statements)

References 42 publications

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“…In E. coli, a single enzyme encoded by cysG catalyzes all three reactions (Stroupe et al 2003), while in yeast, this transformation requires two enzymes: Met1p (a Urogen III methyltransferase) and Met8p (a bifunctional dehydrogenase and sirohydrochlorin FeCh) (Schubert et al 2002). In bacteria, SAM-dependent Urogen III methyltransferase is identified from eubacteria (Blanche et al 1989) and Archae (Blanche et al 1991). In some bacteria including Bacilus megaterium, the transformation of dihydrosirohydrochlorin (precorrin-2) into siroheme is catalyzed by two separate enzymes called SirC (dihydrosirohydrochlorin dehydro-genase) and SirB (sirohydrochlorin ferrochelatase) (Johansson and Hederstedt 1999;Raux et al 2003).…”

Section: Siroheme Branchmentioning

confidence: 99%

Tetrapyrrole Metabolism inArabidopsis thaliana

Tanaka

Kobayashi²,

Masuda

2011

The Arabidopsis Book

217

232

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This manuscript is dedicated to Prof. Mamoru Mimuro of Kyoto University who passed away in Februay 2011.Higher plants produce four classes of tetrapyrroles, namely, chlorophyll (Chl), heme, siroheme, and phytochromobilin. In plants, tetrapyrroles play essential roles in a wide range of biological activities including photosynthesis, respiration and the assimilation of nitrogen/sulfur. All four classes of tetrapyrroles are derived from a common biosynthetic pathway that resides in the plastid. In this article, we present an overview of tetrapyrrole metabolism in Arabidopsis and other higher plants, and we describe all identified enzymatic steps involved in this metabolism. We also summarize recent findings on Chl biosynthesis and Chl breakdown. Recent advances in this field, in particular those on the genetic and biochemical analyses of novel enzymes, prompted us to redraw the tetrapyrrole metabolic pathways. In addition, we also summarize our current understanding on the regulatory mechanisms governing tetrapyrrole metabolism. The interactions of tetrapyrrole biosynthesis and other cellular processes including the plastid-to-nucleus signal transduction are discussed.

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Section: Siroheme Branchmentioning

confidence: 99%

Tetrapyrrole Metabolism inArabidopsis thaliana

Tanaka

Kobayashi²,

Masuda

2011

The Arabidopsis Book

217

232

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“…Plasmid pLMY198, carrying this fragment, restored the ADP-ribosyl acceptor activity of strain LMY12 to nearly the same level as the wild-type strain, FY69 (Fig. 4B) (10), and E. ccli (36), enzymes that methylate the C-2 and C-7 of urogen III in the cobalamin (vitamin B12) biosynthetic pathway (3). The similarities to DPHS are most prominent within residues 1 to 165 and 212 to 254 (Fig.…”

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confidence: 99%

DPH5, a methyltransferase gene required for diphthamide biosynthesis in Saccharomyces cerevisiae.

Mattheakis¹,

Shen²,

Collier³

1992

Mol. Cell. Biol.

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A mutant of Saccharomyces cerevisiae defective in the S-adenosylmethionine (AdoMet)-dependent methyltransferase step of diphthamide biosynthesis was selected by intracellular expression of the F2 fragment of diphtheria toxin (DT) and shown to belong to complementation group DPHS. The DPH5 gene was cloned, sequenced, and found to encode a 300-residue protein with sequence similarity to bacterial AdoMet:uroporphyrinogen Il methyltransferases, enzymes involved in cobalamin (vitamin B12) biosynthesis. Both DPH5 and AdoMet:uroporphyrinogen Ill methyltransferases lack sequence motifs commonly found in other methyltransferases and may represent a new family of AdoMet:methyltransferases. The DPH5 protein was produced in Escherichia coli and shown to be active in methylation of elongation factor 2 partially purified from the dphS mutant. A null mutation of the chromosomal DPHS gene did not affect cell viability, in agreement with other studies indicating that diphthamide is not required for cell survival. The dph5 null mutant survived expression of three enzymically attenuated DT fragments but was killed by expression of fuly active DT fragment A. Consistent with these results, elongation factor 2 from the dph5 null mutant was found to have weak ADP-ribosyl acceptor activity, which was detectable only in the presence of high concentrations of fragment A.

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“…The methyl groups of the four modified amino acids derive from methionine, almost certainly by way of SAM (211). Moreover, SAM is involved in methyl transfer to uroporphyrinogen III in Methanobacterium ivanovii (28) and in the biosynthesis of the methylated pterin in methanopterins in M. formicicum and Methanococcus volta (247).…”

mentioning

confidence: 99%

Microbial Methylation of Metalloids: Arsenic, Antimony, and Bismuth

Bentley

Chasteen

2002

Microbiol Mol Biol Rev

513

316

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A significant 19th century public health problem was that the inhabitants of many houses containing wallpaper decorated with green arsenical pigments experienced illness and death. The problem was caused by certain fungi that grew in the presence of inorganic arsenic to form a toxic, garlic-odored gas. The garlic odor was actually put to use in a very delicate microbiological test for arsenic. In 1933, the gas was shown to be trimethylarsine. It was not until 1971 that arsenic methylation by bacteria was demonstrated. Further research in biomethylation has been facilitated by the development of delicate techniques for the determination of arsenic species. As described in this review, many microorganisms (bacteria, fungi, and yeasts) and animals are now known to biomethylate arsenic, forming both volatile (e.g., methylarsines) and nonvolatile (e.g., methylarsonic acid and dimethylarsinic acid) compounds. The enzymatic mechanisms for this biomethylation are discussed. The microbial conversion of sodium arsenate to trimethylarsine proceeds by alternate reduction and methylation steps, with S-adenosylmethionine as the usual methyl donor. Thiols have important roles in the reductions. In anaerobic bacteria, methylcobalamin may be the donor. The other metalloid elements of the periodic table group 15, antimony and bismuth, also undergo biomethylation to some extent. Trimethylstibine formation by microorganisms is now well established, but this process apparently does not occur in animals. Formation of trimethylbismuth by microorganisms has been reported in a few cases. Microbial methylation plays important roles in the biogeochemical cycling of these metalloid elements and possibly in their detoxification. The wheel has come full circle, and public health considerations are again important

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Purification, characterization, and molecular cloning of S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase from Methanobacterium ivanovii

Cited by 48 publications

References 42 publications

Tetrapyrrole Metabolism inArabidopsis thaliana

Tetrapyrrole Metabolism inArabidopsis thaliana

DPH5, a methyltransferase gene required for diphthamide biosynthesis in Saccharomyces cerevisiae.

Microbial Methylation of Metalloids: Arsenic, Antimony, and Bismuth

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