A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1834, Issue 1, 2013, Pages 380-386

  Park, Jong Tae ^a   Song, Hyung Nam ^b,c   Jung, Tae Yang ^c   Lee, Myoung Hee ^d   Park, Sung Goo ^c   Woo, Eui Jeon ^c,e   Park, Kwan Hwa ^f  

^a Chungnam National University   (South Korea)

^b Korea University   (South Korea)

^c Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

^d Korea Yakult Co   (South Korea)

^e University of Science and Technology (UST)   (South Korea)

^f Sangmyung University   (South Korea)

Author keywords

GH13 family; Hyperthermophilic enzyme; Maltoheptaose production; Monomer; Substrate specificity

Indexed keywords

ACARBOSE; AMYLASE; CYCLODEXTRIN; GLUTAMIC ACID; GLYCINE; PULLULAN; PYROCOCCUS FURIOSUS THERMOSTABLE AMYLASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; ESCHERICHIA COLI; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PYROCOCCUS FURIOSUS;

ALPHA-AMYLASES; AMINO ACID SUBSTITUTION; ARCHAEAL PROTEINS; CATALYTIC DOMAIN; GLUCOSIDASES; MUTATION, MISSENSE; PYROCOCCUS FURIOSUS;

ARCHAEA; BACTERIA (MICROORGANISMS); PYROCOCCUS FURIOSUS;

EID: 84871714045     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.08.001     Document Type: Article

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