نتایج جستجو برای: active site cavity

تعداد نتایج: 828256  

Journal: :European journal of biochemistry 1995
C Kennes F Pries G H Krooshof E Bokma J Kingma D B Janssen

Haloalkane dehalogenase catalyzes the hydrolytic cleavage of carbon-halogen bonds in short-chain haloalkanes. Two tryptophan residues of the enzyme (Trp125 and Trp175) form a halide-binding site in the active-site cavity, and were proposed to play a role in catalysis. The function of these residues was studied by replacing Trp125 with phenylalanine, glutamine or arginine and Trp175 by glutamine...

Journal: :Journal of the American Chemical Society 2012
Shrinivas Dumbre Adeline Derouaux Eveline Lescrinier André Piette Bernard Joris Mohammed Terrak Piet Herdewijn

The peptidoglycan glycosyltransferases (GTs) are essential enzymes that catalyze the polymerization of glycan chains of the bacterial cell wall from lipid II and thus constitute a validated antibacterial target. Their enzymatic cavity is composed of a donor site for the growing glycan chain (where the inhibitor moenomycin binds) and an acceptor site for lipid II substrate. In order to find lead...

Journal: :The Biochemical journal 1992
J Lamotte-Brasseur F Jacob-Dubuisson G Dive J M Frère J M Ghuysen

In previous studies, several amino acids of the active site of class A beta-lactamases have been modified by site-directed mutagenesis. On the basis of the catalytic mechanism proposed for the Streptomyces albus G beta-lactamase [Lamotte-Brasseur, Dive, Dideberg, Charlier, Frère & Ghuysen (1991) Biochem. J. 279, 213-221], the influence that these mutations exert on the hydrogen-bonding network ...

Journal: :polyolefins journal 2015
toshiaki taniike keisuke goto minoru terano

heterogeneous ziegler-natta and homogeneous metallocene catalysts exhibit greatly different active sitenature in olefin polymerization. in our previous study, it was reported that mgcl2-supported titanocenecatalysts can generate both ziegler-natta-type and metallocene-type active sites according to the type of activators.the dual active site nature of the supported titanocene catalysts was furt...

Journal: Polyolefins Journal 2015

Heterogeneous Ziegler-Natta and homogeneous metallocene catalysts exhibit greatly different active sitenature in olefin polymerization. In our previous study, it was reported that MgCl2-supported titanocenecatalysts can generate both Ziegler-Natta-type and metallocene-type active sites according to the type of activators.The dual active site nature of the supported titanocene catalysts was furt...

2013
I. Ahmad Mirza David L. Burk Bing Xiong Hiroaki Iwaki Yoshie Hasegawa Stephan Grosse Peter C. K. Lau Albert M. Berghuis

Cyclohexylamine oxidase (CHAO) is a flavoprotein first described in Brevibacterium oxydans strain IH-35A that carries out the initial step of the degradation of the industrial chemical cyclohexylamine to cyclohexanone. We have cloned and expressed in Escherichia coli the CHAO-encoding gene (chaA) from B. oxydans, purified CHAO and determined the structures of both the holoenzyme form of the enz...

2016
Young-Sik Sohn Seong-Gyu Lee Kwang-Hoon Lee Bonsu Ku Ho-Chul Shin Sun-Shin Cha Yeon-Gil Kim Hyun Sook Lee Sung-Gyun Kang Byung-Ha Oh

A hypothetical protein TON_0340 of a Thermococcus species is a protein conserved in a variety of organisms including human. Herein, we present four different crystal structures of TON_0340, leading to the identification of an active-site cavity harboring a metal-binding site composed of six invariant aspartate and glutamate residues that coordinate one to three metal ions. Biochemical and mutat...

Journal: :Biochemical Society transactions 1995
G Smulevich

Peroxidases are haem-containing enzymes which catalyse the reduction of hydrogen peroxide by different organic substrates. Plant, fungal and bacterial peroxidases are evolutionarily related and constitute the plant peroxidase superfamily, which can be divided into three structural classes. Class I, of prokaryotic origin, includes cytochrome c peroxidase (CCP); class I1 contains secretory fungal...

Journal: :Biochemical Society transactions 2005
S Oliaro-Bosso T Schulz-Gasch S Taramino M Scaldaferri F Viola G Balliano

Substrate access to the active-site cavity of squalene-hopene cyclase from Alicyclobacillus acidocaldarious and lanosterol synthase [OSC (oxidosqualene cyclase)] from Saccharomyces cerevisiae was studied by an inhibition, mutagenesis and homology-modelling approach. Crystal structure and homology modelling indicate that both enzymes possess a narrow constriction that separates an entrance lipop...

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