A novel domain arrangement in a monomeric cyclodextrin ...

PFTA is a unique hyperthermophilic amylase with cyclodextrin hydrolysis activity. The crystal structure of PFTA shows that the enzyme is a self-sufficient ...

A novel domain arrangement in a monomeric cyclodextrin ... - PubMed

PFTA (Pyrococcus furiosus thermostable amylase) is a hyperthermophilic amylase isolated from the archaeon Pyrococcus furiosus.

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A novel domain arrangement in a monomeric cyclodextrin ... - Wikidata

A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus (English). 0 references.

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A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosusBiochimica et ...

Association of Novel Domain in Active Site of Archaic ...

... domain arrangement that combines all of the substrate binding components within a monomeric subunit. ... monomer with a hypothetical cyclodextrin molecule ...

Cyclodextrin-preferring glycoside hydrolases: properties and ...

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

Association of novel domain in active site of archaic ... - PubMed

... cyclodextrin-hydrolyzing enzymes ... domain arrangement that combines all of the substrate binding components within a monomeric subunit.

CATH Domain 4aefB03

A Novel Domain Arrangement in a Monomeric Cyclodextrin-Hydrolyzing Enzyme from the Hyperthermophile Pyrococcus Furiosus. Park, J.-T., Song, H.-N., Jung, T ...

Reference to 3.2.1.54; Id = 721746 - BRENDA Enzyme Database ...

A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus (2013), Biochim. Biophys. Acta, 1834 ...

Carbohydrate Binding Module Family 48 - CAZypedia

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

Cyclodextrin-preferring glycoside hydrolases - De Gruyter

E.J., et al., A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile. Pyrococcus furiosus. Biochim. Biophys ...

Mining for novel cyclomaltodextrin glucanotransferases unravels the ...

Structure of cyclodextrin ... Characterization of an archaeal cyclodextrin glucanotransferase with a novel C-terminal domain.

Jong-Tae Park - Google Scholar

A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus. JT Park, HN Song, TY Jung, MH Lee ...

Glycoside hydrolases from (hyper)thermophilic archaea: structure ...

A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus . Biochim. Biophys. Acta. 1834. ,. 380.

Hydrolysis pattern of α-cyclodextrin (a), β-cyclodextrin (b), and...

... a novel domain arrangement that combines all of the substrate binding components within a monomeric subunit. The SMMA structure provides a molecular basis ...

Structural background of cyclodextrin–protein interactions

... monomer–monomer interaction domain of insulin. By placing a hydrophilic 'cap' on aromatic residues exposed in the monomer but buried in the dimer interface ...

Modulation of the Multisubstrate Specificity of Thermus Maltogenic ...

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

Binding Specificity of a Novel Cyclo/Maltodextrin-Binding Protein ...

mathranii (ThmA) with the crystallographic structure of the three-domain CGTase from C. subterraneus (CldA, PBD ID: 6WNI, sequence identity ...

Association of Novel Domain in Active Site of Archaic ... - OUCI

A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus. Jong-Tae Park, Hyung-Nam Song, Tae ...