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Literature summary for 4.2.2.3 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
Search for more literature for 4.2.2.3

Crystallization (Commentary)

Crystallization (Comment) Organism
recombinant Sphingomonas sp.

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Sphingomonas sp.
-
 A1
-

Substrates and Products (Substrate)

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

Synonyms

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

Ki Value [mM]

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