PMID- 20149347
OWN - NLM
STAT- MEDLINE
DCOM- 20100623
LR  - 20151119
IS  - 1873-426X (Electronic)
IS  - 0008-6215 (Linking)
VI  - 345
IP  - 6
DP  - 2010 Apr 19
TI  - An arginyl residue in rice UDP-arabinopyranose mutase is required for catalytic 
      activity and autoglycosylation.
PG  - 787-91
LID - 10.1016/j.carres.2010.01.008 [doi]
AB  - Plants use UDP-arabinofuranose (UDP-Araf) to donate Araf residues in the 
      biosynthesis of Araf-containing complex carbohydrates. UDP-Araf itself is formed 
      from UDP-arabinopyranose (UDP-Arap) by UDP-arabinopyranose mutase (UAM). However, 
      the mechanism by which this enzyme catalyzes the interconversion of UDP-Arap and 
      UDP-Araf has not been determined. To gain insight into this reaction, 
      functionally recombinant rUAMs were reacted with UDP-Glc or UDP-Araf. The 
      glycosylated recombinant UAMs were fragmented with trypsin, and the glycopeptides 
      formed were then identified and sequenced by LC-MS/MS. The results of these 
      experiments, together with site-directed mutagenesis studies, suggest that in 
      functional UAMs an arginyl residue is reversibly glycosylated with a single 
      glycosyl residue, and that this residue is required for mutase activity. We also 
      provide evidence that a DXD motif is required for catalytic activity.
CI  - Copyright (c) 2010 Elsevier Ltd. All rights reserved.
FAU - Konishi, Tomoyuki
AU  - Konishi T
AD  - Forestry and Forest Products Research Institute, Tsukuba, Ibaraki, Japan.
FAU - Ohnishi-Kameyama, Mayumi
AU  - Ohnishi-Kameyama M
FAU - Funane, Kazumi
AU  - Funane K
FAU - Miyazaki, Yasumasa
AU  - Miyazaki Y
FAU - Konishi, Teruko
AU  - Konishi T
FAU - Ishii, Tadashi
AU  - Ishii T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20100118
PL  - Netherlands
TA  - Carbohydr Res
JT  - Carbohydrate research
JID - 0043535
RN  - 0 (Plant Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Uridine Diphosphate Sugars)
RN  - 14697-41-7 (uridine diphosphate arabinose)
RN  - 94ZLA3W45F (Arginine)
RN  - EC 5.4.- (Intramolecular Transferases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Arginine/genetics/*physiology
MH  - Chromatography, Liquid
MH  - Escherichia coli/genetics/metabolism
MH  - Glycosylation
MH  - Intramolecular Transferases/chemistry/genetics/*metabolism
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Oryza/*enzymology
MH  - Plant Proteins/chemistry/genetics/*metabolism
MH  - Recombinant Proteins/genetics/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH  - Uridine Diphosphate Sugars/*metabolism
EDAT- 2010/02/13 06:00
MHDA- 2010/06/24 06:00
CRDT- 2010/02/13 06:00
PHST- 2009/11/18 00:00 [received]
PHST- 2010/01/05 00:00 [revised]
PHST- 2010/01/11 00:00 [accepted]
PHST- 2010/02/13 06:00 [entrez]
PHST- 2010/02/13 06:00 [pubmed]
PHST- 2010/06/24 06:00 [medline]
AID - S0008-6215(10)00021-2 [pii]
AID - 10.1016/j.carres.2010.01.008 [doi]
PST - ppublish
SO  - Carbohydr Res. 2010 Apr 19;345(6):787-91. doi: 10.1016/j.carres.2010.01.008. Epub 
      2010 Jan 18.