The One-carbon Carrier Methylofuran from Methylobacterium extorquens AM1 Contains a Large Number of α- and γ-Linked Glutamic Acid Residues-Reference-Cited by-同舟云学术

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The One-carbon Carrier Methylofuran from Methylobacterium extorquens AM1 Contains a Large Number of α- and γ-Linked Glutamic Acid Residues

Published:2016-04 Issue:17 Volume:291 Page:9042-9051
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Hemmann Jethro L.,Saurel Olivier,Ochsner Andrea M.,Stodden Barbara K.,Kiefer Patrick,Milon Alain,Vorholt Julia A.

Funder

Eidgenössische Technische Hochschule Zürich

Centre National de la Recherche Scientifique

Max-Planck-Gesellschaft

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference38 articles.

1. Carbon dioxide reduction factor and methanopterin, two coenzymes required for CO2 reduction to methane by extracts of Methanobacterium;Leigh;J. Biol. Chem,1983

2. Structure of methanofuran, the carbon dioxide reduction factor of Methanobacterium thermoautotrophicum;Leigh;J. Am. Chem. Soc,1984

3. Structural elements of methanopterin, a novel pterin;Keltjens;Eur. J. Biochem,1983

4. Tetrahydromethanopterin, a carbon carrier in methanogenesis;Escalante-Semerena;J. Biol. Chem,1984

5. Structure and methylation of coenzyme M (HSCH2CH2SO3);Taylor;J. Biol. Chem,1974

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1. A metabolic puzzle: Consumption of C1 compounds and thiosulfate in Hyphomicrobium denitrificans XT;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2023-01

2. S-Adenosylmethionine (SAM)-Dependent Methyltransferase MftM is Responsible for Methylation of the Redox Cofactor Mycofactocin;ACS Chemical Biology;2022-10-26

3. Structural diversity of the coenzyme methylofuran and identification of enzymes for the biosynthesis of its polyglutamate side chain;Journal of Biological Chemistry;2021-01

4. Structural Basis of Hydrogenotrophic Methanogenesis;Annual Review of Microbiology;2020-09-08

5. Methylofuran is a prosthetic group of the formyltransferase/hydrolase complex and shuttles one-carbon units between two active sites;Proceedings of the National Academy of Sciences;2019-11-27

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