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Literature summary for 2.4.1.129 extracted from

  • Barrett, D.S.; Chen, L.; Litterman, N.K.; Walker, S.
    Expression and characterization of the isolated glycosyltransferase module of Escherichia coli PBP1b (2004), Biochemistry, 43, 12375-12381.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression and characterization of the glycosyltransferase module of PBP1b. The isolated module can be overexpressed at significantly higher levels than the full-length protein Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information turnover-numbers of truncated variants Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ enhances activity of full-length enzyme and truncated variants Escherichia coli
Mg2+ enhances activity of full-length enzyme and truncated variants Escherichia coli
Mn2+ enhances activity of full-length enzyme and truncated variants Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
isolated glycosyltransferase module of PBP1b
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Synonyms

Synonyms Comment Organism
PBP1b
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information turnover-numbers of truncated variants Escherichia coli