Exemplar Abstract for Methanococcus thermolithotrophicus Huber et al. 1984 and Methanothermococcus thermolithotrophicus (Huber et al. 1984) Whitman 2002.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  
Methanococcus Thermolithotrophicus

scholarly journals Biochemical and Genetic Characterization of an FK506-Sensitive Peptidyl Prolyl cis-trans Isomerase from a Thermophilic Archaeon, Methanococcus thermolithotrophicus

1998 ◽  
Vol 180 (2) ◽  
pp. 388-394 ◽  
Author(s):  
Masahiro Furutani ◽  
Toshii Iida ◽  
Shigeyuki Yamano ◽  
Kei Kamino ◽  
Tadashi Maruyama
Keyword(s):  
Amino Acid ◽  
Genomic Library ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Ppiase Activity ◽  
Methanococcus Thermolithotrophicus ◽  
Fk506 Binding Protein ◽  
Thermophilic Archaeon

ABSTRACT A peptidyl prolyl cis-trans isomerase (PPIase) was purified from a thermophilic methanogen, Methanococcus thermolithotrophicus. The PPIase activity was inhibited by FK506 but not by cyclosporine. The molecular mass of the purified enzyme was estimated to be 16 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 42 kDa by gel filtration. The enzyme was thermostable, with the half-lives of its activity at 90 and 100°C being 90 and 30 min, respectively. The catalytic efficiencies (k cat/Km ) measured at 15°C for the peptidyl substrates,N-succinyl-Ala-Leu-Pro-Phe-p-nitroanilide andN-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, were 0.35 and 0.20 μM−1 s−1, respectively, in chymotrypsin-coupled assays. The purified enzyme was sensitive to FK506 and therefore was called MTFK (M. thermolithotrophicusFK506-binding protein). The MTFK gene (462 bp) was cloned from anM. thermolithotrophicus genomic library. The comparison of the amino acid sequence of MTFK with those of other FK506-binding PPIases revealed that MTFK has a 13-amino-acid insertion in the N-terminal region that is unique to thermophilic archaea. The relationship between the thermostable nature of MTFK and its structure is discussed.

scholarly journals FK506 Binding Protein from a Thermophilic Archaeon,Methanococcus thermolithotrophicus, Has Chaperone-like Activity in Vitro

Biochemistry ◽  
2000 ◽  
Vol 39 (10) ◽  
pp. 2822-2822 ◽  
Author(s):  
Masahiro Furutani ◽  
Akira Ideno ◽  
Toshii Iida ◽  
Tadashi Maruyama
Keyword(s):  
Binding Protein ◽  
Methanococcus Thermolithotrophicus ◽  
Fk506 Binding Protein ◽  
Thermophilic Archaeon

scholarly journals Group II Chaperonin in a Thermophilic Methanogen,Methanococcus thermolithotrophicus

1998 ◽  
Vol 273 (43) ◽  
pp. 28399-28407 ◽  
Author(s):  
Masahiro Furutani ◽  
Toshii Iida ◽  
Takao Yoshida ◽  
Tadashi Maruyama
Keyword(s):  
Methanococcus Thermolithotrophicus ◽  
Group Ii ◽  
Group Ii Chaperonin
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