ISSN:
1432-072X
Keywords:
Key words Formyltransferase
;
Formyltetrahydrofolate
;
synthase
;
Hyperthermophilic enzymes
;
Methanogenic
;
Archaea
;
Methanosarcina barkeri
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract The ftr gene encoding formylmethanofuran: tetrahydromethanopterin formyltransferase (Ftr) from Methanosarcina barkeri was cloned, sequenced, and functionally expressed in Escherichia coli. The overproduced enzyme was purified eightfold to apparent homogeneity, and its catalytic properties were determined. The primary structure and the hydropathic character of the formyltransferase from Methanosarcina barkeri were compared with those of the enzymes from Methanobacterium thermoautotrophicum, Methanothermus fervidus, and Methanopyrus kandleri. The amino acid sequence of the enzyme from Methanosarcina barkeri was 64%, 61%, and 59% identical to that of the enzyme from Methanobacterium thermoautotrophicum, Methanothermus fervidus, and Methanopyrus kandleri, respectively. A negative correlation between the hydrophobicity of the enzymes and both the growth temperature optimum and the intracellular salt concentration of the four organisms was observed. The hydrophobicity of amino acid composition was +21.6 for the enzyme from Methanosarcina barkeri (growth temperature optimum 37° C, intracellular salt concentration ≈ 0.3 M), +9.9 for the enzyme from Methanobacterium thermoautotrophicum (65°C, ≈ 0.7 M), –20.8 for the enzyme from Methanothermus fervidus (83° C, ≈ 1.0 M) and –31.4 for the enzyme from Methanopyrus kandleri (98° C, 〉 1.1 M). Generally, a positive correlation between hydrophobicity and thermophilicity of enzymes and a negative correlation between hydrophobicity and halophilicity of enzymes are observed. The findings therefore indicate that the hydropathic character of the formyltransferases compared is mainly determined by the intracellular salt concentration rather than by temperature. Sequence similarities between the formyltransferases from methanogens and an open reading frame from Methylobacterium extorquens AM1 are discussed.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s002030050303
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