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

BRENDA support

Literature summary for 4.2.2.3 extracted from

  • Qin, H.M.; Miyakawa, T.; Inoue, A.; Nishiyama, R.; Nakamura, A.; Asano, A.; Ojima, T.; Tanokura, M.
    Structural basis for controlling the enzymatic properties of polymannuronate preferred alginate lyase FlAlyA from the PL-7 family (2018), Chem. Commun. (Camb.), 54, 555-558 .
    View publication on PubMed
Search for more literature for 4.2.2.3

Crystallization (Commentary)

Crystallization (Comment) Organism
structure at 1.54 A resolution and modeling of binding of 4-deoxy-alpha-L-erythro-hex-4-enuronosyl-Gluc-Man-Gluc and Man-Gluc-Man Flavobacterium sp. UMI-01

Protein Variants

Protein Variants Comment Organism
D139A mutation in subsite +2, decrease in activity Flavobacterium sp. UMI-01
K158F increase in activity under acidic conditions Flavobacterium sp. UMI-01
K158H increase in activity under acidic conditions Flavobacterium sp. UMI-01
K158L increase in activity under acidic conditions Flavobacterium sp. UMI-01
K158N increase in activity under acidic conditions Flavobacterium sp. UMI-01
K158W mutation increases the liberation of disaccharides and 4-deoxy-L-erythro-5-hexoseulose uronic acid but does not show complete exolytic activity. Decrease in optimum pH value Flavobacterium sp. UMI-01
K158Y increase in activity under acidic conditions Flavobacterium sp. UMI-01
S28D no change in specific activity toward alginate Flavobacterium sp. UMI-01
S28E no change in specific activity toward alginate Flavobacterium sp. UMI-01
T12K mutation in subsite +3, decrease in activity Flavobacterium sp. UMI-01
T12K/T14Q/S28E/T70S/D139A mutation does not improve the poly(G) preference compared to wild-type Flavobacterium sp. UMI-01
T12R mutation in subsite +3, decrease in activity Flavobacterium sp. UMI-01
T14Q/N mutation in subsite +3, decrease in activity Flavobacterium sp. UMI-01
T70S no change in specific activity toward alginate Flavobacterium sp. UMI-01
T70S/D139A mutation decreases the relative activity of poly(alpha-1,4-L guluronate) toward poly(beta-1,4-D-mannuronate) Flavobacterium sp. UMI-01
Y233F mutant shows an increase in the relative activity of poly(alpha-1,4-L guluronate) or poly(alpha-1,4-L guluronate)/(beta-1,4-D-mannuronate) toward poly(beta-1,4-D-mannuronate) Flavobacterium sp. UMI-01
Y233F mutation in subsite +2, decrease in activity Flavobacterium sp. UMI-01

Organism

Organism UniProt Comment Textmining
Flavobacterium sp. UMI-01 A0A068PC91
-
-

Synonyms

Synonyms Comment Organism
AlyA
-
 Flavobacterium sp. UMI-01

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 6.8 mutant K158W Flavobacterium sp. UMI-01
6.8 8 wild-type Flavobacterium sp. UMI-01