Open AccessEvidence that participate methane monooxygenase and ammonia monooxygenase may be evolutionarily related
Author(s) -
Holmes Andrew J.,
Costello Andria,
Lidstrom Mary E.,
Murrell J. Colin
Publication year - 1995
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1995.tb07834.x
Subject(s) - ammonia monooxygenase , methane monooxygenase , monooxygenase , biology , biochemistry , bacteria , proteobacteria , methanotroph , gene , amino acid , peptide sequence , genetics , microbiology and biotechnology , enzyme , anaerobic oxidation of methane , 16s ribosomal rna , cytochrome p450 , archaea , catalysis
Genes encoding paniculate methane monooxygenase and ammonia monooxygenase share high sequence identity. Degenerate oligonucleotide primers were designed, based on regions of shared amino acid sequence between the 27‐kDa polypeptides, which are believed to contain the active sites, of particulate methane monooxygenase and ammonia monooxygenase. A 525‐bp internal DNA fragment of the genes encoding these polypeptides ( pmoA and amoA ) from a variety of methanotrophic and nitrifying bacteria was amplified by PCR, cloned and sequenced. Representatives of each of the phylogenetic groups of both methanotrophs (α‐ and γ‐Proteobacteria) and ammonia‐oxidizing nitrifying bacteria (β‐and y‐Proteobacteria) were included. Analysis of the predicted amino acid sequences of these genes revealed strong conservation of both primary and secondary structure. Nitrosococcus oceanus AmoA showed higher identity to PmoA sequences from other members of the γ‐Proteobacteria than to AmoA sequences. These results suggest that the particulate methane monooxygenase and ammonia monooxygenase are evolutionarily related enzymes despite their different physiological roles in these bacteria.