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Literature summary extracted from

  • Akhtar, M.S.; Bhakuni, V.
    Role of ionic interactions and linker in the domain interaction and modulation of functional activity of hyaluronate lyases (2007), Biochem. Biophys. Res. Commun., 353, 286-292.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.2.1 cloning, overexpression and purification of the C-terminal domain swapped chimeras of SpnHL and SagHL (hyaluronate lyase from Streptococcus agalactiae), modified enzyme SpnHLv/SagHLv (where the size of linker connecting the alpha-domain to C-terminal domain is enlarged by two amino acid) Streptococcus pneumoniae

Protein Variants

EC Number Protein Variants Comment Organism
4.2.2.1 additional information C-terminal domain swapped chimeras of SpnHL and SagHL, modified enzyme SpnHLv/SagHLv (where the size of linker connecting the alpha-domain to C-terminal domain is enlarged by two amino acid) Streptococcus pneumoniae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.2.1 additional information
-
 additional information Km-values of C-terminal domain swapped chimeras of SpnHL and SagHL, modified enzyme SpnHLv/SagHLv (where the size of linker connecting the alpha-domain to C-terminal domain is enlarged by two amino acid) Streptococcus pneumoniae

Organism

EC Number Organism UniProt Comment Textmining
4.2.2.1 Streptococcus pneumoniae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.2.1 cloning, overexpression and purification of the C-terminal domain swapped chimeras of SpnHL and SagHL, modified enzyme SpnHLv/SagHLv (where the size of linker connecting the alpha-domain to C-terminal domain is enlarged by two amino acid) Streptococcus pneumoniae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.2.1 additional information C-terminal domain does not bind directly to the substrate, instead the domain contributes to the interaction with the polymeric hyaluronan for catalysis. Furthermore, the substrate specificity exchanges with the size of catalytic cleft. The role of linker connecting alpha-domain to C-terminal domain is found to hold the C-terminal domain in a conformation suitable for achieving maximum activity Streptococcus pneumoniae ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.2.1 spnHL
-
 Streptococcus pneumoniae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.2.1 additional information
-
 additional information turnover numbers of C-terminal domain swapped chimeras of SpnHL and SagHL, modified enzyme SpnHLv/SagHLv (where the size of linker connecting the alpha-domain to C-terminal domain is enlarged by two amino acid) Streptococcus pneumoniae