Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other

Journal of Biological Chemistry

Volumn 277, Issue 24, 2002, Pages 21891-21897

  Lee, Hee Seob ^a,b,c,d   Kim, Min Sung ^a,b,c,d   Cho, Hyun Soo ^a,b,c,d   Kim, Jung In ^a,b,c,d   Kim, Tae Jip ^a,b,c,d   Choi, Ji Hye ^a,b,c,d   Park, Cheonseok ^a,b,c,d   Lee, Heung Soo ^a,b,c,d   Oh, Byung Ha ^a,b,c,d   Park, Kwan Hwa ^a,b,c,d  

^a Pohang University of Science and Technology (POSTECH)   (South Korea)

^b POSTECH   (South Korea)

^c Seoul National University   (South Korea)

^d Kyung Hee University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME CODES;

BACTERIA; DATABASE SYSTEMS; MOLECULAR STRUCTURE; NUCLEIC ACID SEQUENCES;

ENZYMES;

AMYLASE; CYCLOMALTODEXTRIN GLUCANOTRANSFERASE; CYCLOMALTODEXTRINASE; MALTOGENIC AMYLASE; NEOPULLULANASE; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS; CIRCULAR DICHROISM; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME ASSAY; ENZYME SPECIFICITY; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN PURIFICATION; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; THERMUS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BACILLUS; BINDING SITES; CATALYSIS; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; DEXTRINS; DIMERIZATION; GLYCOSIDE HYDROLASES; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PHENYLALANINE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY; THERMUS; TIME FACTORS; TRYPTOPHAN;

BACILLUS SP.; BACILLUS SP. I-5; BACTERIA (MICROORGANISMS); THERMUS;

EID: 0037077228     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M201623200     Document Type: Article

References (24)