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

BRENDA support

Literature summary extracted from

  • Yamasaki, M.; Ogura, K.; Hashimoto, W.; Mikami, B.; Murata, K.
    A structural basis for depolymerization of alginate by polysaccharide lyase family-7 (2005), J. Mol. Biol., 352, 11-21.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.2.3 recombinant Sphingomonas sp.

Protein Variants

EC Number Protein Variants Comment Organism
4.2.2.3 E148A mutant protein is insoluble Sphingomonas sp.
4.2.2.3 H191A Vmax is 7230fold lower than wild-type value Sphingomonas sp.
4.2.2.3 K280A Vmax is 243fold lower than wild-type value Sphingomonas sp.
4.2.2.3 Q189A Vmax is 185080fold lower than wild-type value Sphingomonas sp.
4.2.2.3 R146A Vmax is 193fold lower than wild-type value Sphingomonas sp.
4.2.2.3 R150A Vmax is 2103fold lower than wild-type value Sphingomonas sp.
4.2.2.3 Y278F Vmax is 1.3fold higher than wild-type value Sphingomonas sp.
4.2.2.3 Y284F Vmax is 308fold lower than wild-type value Sphingomonas sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.2.3 (NH4)2SO4 competitive Sphingomonas sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.2.3 additional information
-
additional information
-
Sphingomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
4.2.2.3 Sphingomonas sp.
-
A1
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.2.3 alginate Arg146, Gln189, His191, and Tyr284 form an active center Sphingomonas sp. unsaturated algino-oligosaccharides
-
?

Synonyms

EC Number Synonyms Comment Organism
4.2.2.3 alginate lyase A1-II'
-
Sphingomonas sp.

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.2.2.3 2.5
-
(NH4)2SO4 pH 7.5, 30°C Sphingomonas sp.