C1 transfer enzymes and coenzymes linking methylotrophic bacteria and methanogenic archaea

Science

Volumn 281, Issue 5373, 1998, Pages 99-102

  Chistoserdova, Ludmila ^a   Vorholt, Julia A ^b   Thauer, Rudolf K ^b   Lidstrom, Mary E ^a  

^a University of Washington   (United States)

^b MAX PLANCK INSTITUTE FOR TERRESTRIAL MICROBIOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; DIHYDROFOLATE REDUCTASE; 5,6,7,8 TETRAHYDROMETHANOPTERIN; 5,6,7,8-TETRAHYDROMETHANOPTERIN; FORMYLMETHANOFURAN TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE; FORMYLMETHANOFURAN-TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE; HYDROLASE; METHANOL; METHENYLTETRAHYDROMETHANOPTERIN CYCLOHYDROLASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PTERIN DERIVATIVE; SUCCINIC ACID; TRANSFERASE;

AMINO ACID SEQUENCE; ARTICLE; COENZYME; ENERGY METABOLISM; ENZYME ACTIVITY; EVOLUTION; GENE CLUSTER; METHANOBACTERIUM; METHANOGENESIS; METHYLOBACTERIUM; NONHUMAN; OPEN READING FRAME; PRIORITY JOURNAL; BACTERIAL GENE; BACTERIUM TRANSFORMATION; CHEMISTRY; ENZYMOLOGY; ESCHERICHIA COLI; EURYARCHAEOTA; GENE; GENETICS; GRAM NEGATIVE AEROBIC RODS AND COCCI; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; MUTATION; OXIDATION REDUCTION REACTION; SEQUENCE ALIGNMENT;

ARCHAEA; BACTERIA (MICROORGANISMS); METHANOBACTERIUM; METHYLOBACTERIUM;

AMINO ACID SEQUENCE; AMINOHYDROLASES; ESCHERICHIA COLI; EURYARCHAEOTA; EVOLUTION; GENES, ARCHAEAL; GENES, BACTERIAL; GRAM-NEGATIVE AEROBIC RODS AND COCCI; HYDROXYMETHYL AND FORMYL TRANSFERASES; METHANOL; MOLECULAR SEQUENCE DATA; MUTATION; NAD; NADP; OXIDATION-REDUCTION; PTERINS; SEQUENCE ALIGNMENT; SUCCINIC ACID; TRANSFORMATION, BACTERIAL;

EID: 0032479058     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.281.5373.99     Document Type: Article

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29. We are grateful to A. Springer (University of Washington) for sequencing the region encoding FfsA and Orf3, and to T. Selmer (University of Marburg) for performing the MALDI/TOF mass spectometry analysis. This work was supported in part by a grant from the NIH (GM36296) to M.E.L