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Crystal structure of a lactosucrose-producing enzyme, Arthrobacter sp. K-1 β-fructofuranosidase

Paper ID Volume ID Publish Year Pages File Format Full-Text
17190 42650 2012 7 PDF Available
Title
Crystal structure of a lactosucrose-producing enzyme, Arthrobacter sp. K-1 β-fructofuranosidase
Abstract

Arthrobacter sp. K-1 β-fructofuranosidase (ArFFase), a glycoside hydrolase family 68 enzyme, catalyzes the hydrolysis and transfructosylation of sucrose. ArFFase is useful for producing a sweetener, lactosucrose (4G-β-d-galactosylsucrose). The primary structure of ArFFase is homologous to those of levansucrases, although ArFFase catalyzes mostly hydrolysis when incubated with sucrose alone, even at high concentration. Here, we determined the crystal structure of ArFFase in unliganded form and complexed with fructose. ArFFase consisted of a five-bladed β-propeller fold as observed in levansucrases. The structure of ArFFase was most similar to that of Gluconacetobacter diazotrophicus levansucrase (GdLev). The structure of the catalytic cleft of ArFFase was also highly homologous to that of GdLev. However, two amino acid residues, Tyr232 and Pro442 in ArFFase, were not conserved between them. A tunnel observed at the bottom of the catalytic cleft of ArFFase may serve as a water drain or its reservoir.

► We determined the crystal structure of a GH68 lactosucrose-producing enzyme. ► The structure was most similar to that of Gluconacetobacter levansucrase. ► Tyr232 and Pro442 were not conserved in Gluconacetobacter levansucrase. ► There is a water tunnel from the bottom of the catalytic cleft to the enzyme surface.

Keywords
ArFFase, Arthrobacter sp. K-1 β-fructofuranosidase; BsLev, Bacillus subtilis levansucrase; GdLev, Gluconacetobacter diazotrophicus levansucrase; GH, glycoside hydrolase familyβ-Fructofuranosidase; Levansucrase; Lactosucrose; β-Propeller; Glycoside hydrola
First Page Preview
Crystal structure of a lactosucrose-producing enzyme, Arthrobacter sp. K-1 β-fructofuranosidase
Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 51, Issues 6–7, 10 December 2012, Pages 359–365
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering