An atypical approach identifies TYR234 as the key base catalyst in chondroitin AC lyase.
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Structural and Mutational Characterization of the Catalytic A-module of the Mannuronan C-5-epimerase AlgE4 from Azotobacter vinelandiiStructure of a PL17 Family Alginate Lyase Demonstrates Functional Similarities among Exotype DepolymerasesRmlC, a C3' and C5' carbohydrate epimerase, appears to operate via an intermediate with an unusual twist boat conformationEngineering broad-spectrum digestion of polyuronides from an exolytic polysaccharide lyaseA hierarchical classification of polysaccharide lyases for glycogenomics.Structural and mechanistic classification of uronic acid-containing polysaccharide lyases.Insight into the role of substrate-binding residues in conferring substrate specificity for the multifunctional polysaccharide lyase Smlt1473.
P2860
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P2860
An atypical approach identifies TYR234 as the key base catalyst in chondroitin AC lyase.
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name
An atypical approach identifies TYR234 as the key base catalyst in chondroitin AC lyase.
@en
An atypical approach identifies TYR234 as the key base catalyst in chondroitin AC lyase.
@nl
type
label
An atypical approach identifies TYR234 as the key base catalyst in chondroitin AC lyase.
@en
An atypical approach identifies TYR234 as the key base catalyst in chondroitin AC lyase.
@nl
prefLabel
An atypical approach identifies TYR234 as the key base catalyst in chondroitin AC lyase.
@en
An atypical approach identifies TYR234 as the key base catalyst in chondroitin AC lyase.
@nl
P2093
P2860
P356
P1433
P1476
An atypical approach identifies TYR234 as the key base catalyst in chondroitin AC lyase.
@en
P2093
Allan Matte
Carl S Rye
Miroslaw Cygler
Stephen G Withers
P2860
P304
P356
10.1002/CBIC.200500428
P577
2006-04-01T00:00:00Z