1JF6

Crystal structure of thermoactinomyces vulgaris r-47 alpha-amylase mutant F286Y

Summary for 1JF6

• Entry DOI: 10.2210/pdb1jf6/pdb
• Related: 1BVZ 1JF5
• Descriptor: ALPHA AMYLASE II, CALCIUM ION (2 entities in total)
• Functional Keywords: alpha/beta barrel, hydrolase
• Biological source: Thermoactinomyces vulgaris
• Total number of polymer chains: 2
• Total formula weight: 135220.37

Authors

Ohtaki, A.,Kondo, S.,Shimura, Y.,Tonozuka, T.,Sakano, Y.,Kamitori, S. (deposition date: 2001-06-20, release date: 2002-05-22, Last modification date: 2024-05-29)

Primary citation

Ohtaki, A.,Kondo, S.,Shimura, Y.,Tonozuka, T.,Sakano, Y.,Kamitori, S.
Role of Phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structures of the mutant TVAIIs, F286A and F286Y, and kinetic analyses of the Phe286-replaced mutant TVAIIs
CARBOHYDR.RES., 334:309-313, 2001

PubMed Abstract: Phe286 located in the center of the active site of alpha-amylase 2 from Thermoactinomyces vulgaris R-47 (TVAII) plays an important role in the substrate recognition for cyclomaltooligosaccharides (cyclodextrins). The X-ray structures of mutant TVAIIs with the replacement of Phe286 by Ala (F286A) and Tyr (F286Y) were determined at 3.2 A resolution. Their structures have no significant differences from that of the wild-type enzyme. The kinetic analyses of Phe286-replaced variants showed that the variants with non-aromatic residues, Ala (F286A) and Leu (F286L), have lower enzymatic activities than those with aromatic residues, Tyr (F286Y) and Trp (F286W), and the replacement of Phe286 affects enzymatic activities for CDs more than those for starch.

PubMed: 11527532
DOI: 10.1016/S0008-6215(01)00190-2

Experimental method

X-RAY DIFFRACTION (3.2 Å)