4CGT

DELETION MUTANT DELTA(145-150), F151D OF CYCLODEXTRIN GLYCOSYLTRANSFERASE

Summary for 4CGT

• Entry DOI: 10.2210/pdb4cgt/pdb
• Descriptor: CYCLODEXTRIN GLYCOSYLTRANSFERASE, CALCIUM ION (3 entities in total)
• Functional Keywords: glycosyltransferase, starch degradation, cyclodextrin
• Biological source: Bacillus circulans
• Cellular location: Secreted (By similarity): P30920
• Total number of polymer chains: 1
• Total formula weight: 73948.42

Authors

Parsiegla, G.,Schulz, G.E. (deposition date: 1998-06-06, release date: 1998-08-12, Last modification date: 2024-10-09)

Primary citation

Parsiegla, G.,Schmidt, A.K.,Schulz, G.E.
Substrate binding to a cyclodextrin glycosyltransferase and mutations increasing the gamma-cyclodextrin production.
Eur.J.Biochem., 255:710-717, 1998

PubMed Abstract: Bacterial cyclodextrin glycosyltransferases use starch to produce cyclic maltooligosaccharides (cyclodextrins) which are of interest in various applications. The cyclization reaction gives rise to a spectrum of ring sizes consisting of predominantly six to eight glucosyl units. Using the enzyme from Bacillus circulans strain no. 8, binding studies have been performed with several substrates and analogues. The observed binding modes differ in detail, but agree in general with data on homologous enzymes. Based on these binding studies, two mutations were designed that changed the production spectrum from the predominant product beta-cyclodextrin of the wild-type enzyme towards gamma-cyclodextrin, which is of practical interest because it is rare and can encapsulate larger nonpolar compounds.

PubMed: 9738912
DOI: 10.1046/j.1432-1327.1998.2550710.x

Experimental method

X-RAY DIFFRACTION (2.6 Å)