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GrainGenes Reference Report: FBS-567-214

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Reference
FBS-567-214
Title
The large subunit determines catalytic specificity of barley sucrose:fructan 6-fructosyltransferase and fescue sucrose:sucrose 1-fructosyltransferase
Journal
FEBS Letters
Year
2004
Volume
567
Pages
214-218
Author
Altenbach D
Nuesch E
Meyer AD
Boller T
Wiemken A
Abstract
Plant fructosyltransferases are highly homologous in primary sequence and typically consist of two subunits but catalyze widely different reactions. Using functional expression in the yeast Pichia pastoris, we show that the substrate specificity of festuca sucrose:sucrose 1-D-fructosyltransferase (1-SST) and barley sucrose:fructan 6-D-fructosyltransferase (6-SFT) is entirely determined by the large subunit. Chimeric enzymes with the large subunit of festuca 1-SST (LSuB) and the small subunit of barley 6-SFT have the same catalytic specificity as the native festuca 1-SST and vice versa. If the LSuB is expressed alone, it does not yield a functionally active enzyme, indicating that the small subunit is nevertheless essential
External Databases
Pubmed: 15178325
Keyword
[ Hide all but 1 of 35 ]
6-fructosyltransferase
active enzyme
barley
biochemistry
catalytic activity
cereal enzyme specificity
chicory
cloning
enzyme
enzyme activity
fescue
festuca
fructan
fructan 6-fructosyltransferase
fructosyltransferase
functional expression
hexosyltransferases
large subunit
model
pichia
pichia pastoris
pichia-pastoris
purification
root
sequence
specificity
substrate
substrate specificity
subunit
sucrose
sucrose : fructan 6-beta-d-fructosyltransferase
sucrose : sucrose 1-beta-d-fructosyltransferase
transferase
yeast
yield

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