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Literature summary for 5.3.4.1 extracted from

  • Goo, T.W.; Yun, E.Y.; Kim, S.W.; Choi, K.H.; Kang, S.W.; Shin, K.; Yu, K.; Kwon, O.
    Domain a' of Bombyx mori protein disulfide isomerase has chaperone activity (2008), Z. Naturforsch. C, 63, 435-439.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information expression of full protein, domain a + part of domain b comprised of residues 1-162, parts of domains b + b' comprised of residues 163-315, and part of domain b' + domain a' including c comprised of resiudes 316-494, respectively, in Escherichia coli. Segment 1-162 lacks isomerase activity, while segment 316-494 displays wild-type like activity Bombyx mori

Organism

Organism UniProt Comment Textmining
Bombyx mori Q9GPH2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
reduced RNase A
-
Bombyx mori RNase A
-
?
scrambled RNase A
-
Bombyx mori RNase A
-
?