Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.2.1.8 extracted from

  • Suzuki, R.; Nagata, K.; Yumoto, F.; Kawakami, M.; Nemoto, N.; Furutani, M.; Adachi, K.; Maruyama, T.; Tanokura, M.
    Three-dimensional solution structure of an archaeal FKBP with a dual function of peptidyl prolyl cis-trans isomerase and chaperone-like activities (2003), J. Mol. Biol., 328, 1149-1160.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Methanothermococcus thermolithotrophicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the IF domain is a novel-folding motif and exposes a hydrophobic surface, which is considered to play an important role in the chaperone-like activity Methanothermococcus thermolithotrophicus ?
-
?

Subunits

Subunits Comment Organism
More three-dimensional solution structure. The IF domain is a novel-folding motif and exposes a hydrophobic surface, which is considered to play an important role in the chaperone-like activity Methanothermococcus thermolithotrophicus

Synonyms

Synonyms Comment Organism
MtFKBP17
-
Methanothermococcus thermolithotrophicus