The binding pattern of two carbohydrate-binding modules of laminarinase Lam16A from Thermotoga neapolitana: Differences in β-glucan binding within family CBM4

Microbiology

Volumn 147, Issue 3, 2001, Pages 621-629

  Zverlov, V V ^a   Volkov, I Y ^a   Velikodvorskaya, G A ^a   Schwarz, W H ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

1,3 Glucanase; Binding specificity; Substrate binding module CBM4; Thermotoga neapolitana

Indexed keywords

BACTERIAL ENZYME; BETA 1,3 GLUCAN; BETA GLUCAN; CARBOHYDRATE BINDING PROTEIN; CURDLAN; ENDO 1,3 BETA GLUCANASE; GLYCOSIDASE; LAMINARAN; POLYSACCHARIDE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BARLEY; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; GELATINIZATION; GENE DELETION; HYDROLYSIS; MODULATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FAMILY; SEQUENCE HOMOLOGY; SOLUBILITY; STIMULATION; THERMOSTABILITY; THERMOTOGA; THERMOTOGA NEAPOLITANA; YEAST CELL;

BACTERIA (MICROORGANISMS); HORDEUM VULGARE SUBSP. VULGARE; NEGIBACTERIA; THERMOTOGA; THERMOTOGA NEAPOLITANA;

EID: 0035078068     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-147-3-621     Document Type: Article

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