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Literature summary for 3.1.1.85 extracted from

  • Tomczyk, N.H.; Nettleship, J.E.; Baxter, R.L.; Crichton, H.J.; Webster, S.P.; Campopiano, D.J.
    Purification and characterisation of the BIOH protein from the biotin biosynthetic pathway (2002), FEBS Lett., 513, 299-304.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Hms174(DE3) cells Escherichia coli
expressed in Escherichia coli Hms174(DE3) cells Neisseria meningitidis

Protein Variants

Protein Variants Comment Organism
S53A the mutant is insoluble Escherichia coli
S82A the mutation does not prevent coenzyme A binding Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27040
-
calculated from amino acid sequence Neisseria meningitidis
28000
-
SDS-PAGE Escherichia coli
28000
-
SDS-PAGE Neisseria meningitidis
28510
-
calculated from amino acid sequence Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli JM101
-
-
-
Neisseria meningitidis
-
-
-
Neisseria meningitidis H44/76
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Q-Sepharose column chromatography and gel filtration Escherichia coli
Q-Sepharose column chromatography and gel filtration Neisseria meningitidis

Synonyms

Synonyms Comment Organism
BioH
-
Escherichia coli
BioH
-
Neisseria meningitidis

General Information

General Information Comment Organism
metabolism the bioH gene product is required for the synthesis of pimeloyl-CoA Escherichia coli
metabolism the bioH gene product is required for the synthesis of pimeloyl-CoA Neisseria meningitidis