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Information on EC 2.4.1.281 - 4-O-beta-D-mannosyl-D-glucose phosphorylase and Organism(s) Bacteroides fragilis and UniProt Accession Q5LH68

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.281 4-O-beta-D-mannosyl-D-glucose phosphorylase
IUBMB Comments
This enzyme forms part of a mannan catabolic pathway in the anaerobic bacterium Bacteroides fragilis NCTC 9343.
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This record set is specific for:
Bacteroides fragilis
UNIPROT: Q5LH68
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Word Map
  • 2.4.1.281
  • calcitonin
  • receptor-like
  • adrenomedullin
  • gene-related
  • activity-modifying
  • camp
  • vasodilator
  • amylin
  • endothelial
  • artery
  • neuropeptide
  • receptor-activity-modifying
  • migraine
  • protein-coupled
  • calcitonin-receptor-like
  • cgrp-induced
  • intermedin
  • gpcrs
  • calcitonin-like
  • cgrp-mediated
  • trigeminovascular
  • bibn4096bs
  • trigeminal
  • calcitonin-gene-related
  • receptor-activity
  • hypotensive
  • cgrp-receptors
  • am-induced
  • calcrl
The taxonomic range for the selected organisms is: Bacteroides fragilis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
ramp1, ramp2, bf0772, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
4-O-beta-D-mannopyranosyl-D-glucopyranose:phosphate alpha-D-mannosyltransferase
This enzyme forms part of a mannan catabolic pathway in the anaerobic bacterium Bacteroides fragilis NCTC 9343.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-O-beta-D-mannopyranosyl-D-glucopyranose + phosphate
D-glucose + alpha-D-mannose 1-phosphate
show the reaction diagram
phosphorolysis reaction
-
-
r
additional information
?
-
no substrates are 4-O-beta-D-xylopyranosyl-D-xylose, sophorose, sucrose, laminaribiose, cellobiose, lactose, epilactose, 4-O-beta-D-mannopyranosyl-D-mannose, gentiobiose, kojibiose, nigerose, maltose, isomaltose.
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-O-beta-D-mannopyranosyl-D-glucopyranose + phosphate
D-glucose + alpha-D-mannose 1-phosphate
show the reaction diagram
phosphorolysis reaction
-
-
r
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.3
4-O-beta-D-mannopyranosyl-D-glucopyranose
pH 7.5, 30°C
2
phosphate
pH 7.5, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
42.2
4-O-beta-D-mannopyranosyl-D-glucopyranose
pH 7.5, 30°C
24.8
phosphate
pH 7.5, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.1
4-O-beta-D-mannopyranosyl-D-glucopyranose
pH 7.5, 30°C
12.4
phosphate
pH 7.5, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28.5
pH 7.5, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43890
calculated from amino acid sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.68 A resolution. The enzyme shows a homohexameric structure, which is formed by using two helices attached to the N-terminus and C-terminus as a tab for sticking between subunits. In complexes with substrates, 4-O-beta-D-mannosyl-D-glucose and phosphate, and the product D-mannose-1-phosphate the structures reveal that the invariant residue Asp131, is supposed to be the general acid/base, does not exist close to the glycosidic Glc-O4 atom, which should be protonated in the catalytic reaction
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Senoura, T.; Ito, S.; Taguchi, H.; Higa, M.; Hamada, S.; Matsui, H.; Ozawa, T.; Jin, S.; Watanabe, J.; Wasaki, J.; Ito, S.
New microbial mannan catabolic pathway that involves a novel mannosylglucose phosphorylase
Biochem. Biophys. Res. Commun.
408
701-716
2011
Bacteroides fragilis (Q5LH68)
Manually annotated by BRENDA team
Nakae, S.; Ito, S.; Higa, M.; Senoura, T.; Wasaki, J.; Hijikata, A.; Shionyu, M.; Ito, S.; Shirai, T.
Structure of novel enzyme in mannan biodegradation process 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP
J. Mol. Biol.
425
4468-4478
2013
Bacteroides fragilis (Q5LH68), Bacteroides fragilis DSM 2151 (Q5LH68)
Manually annotated by BRENDA team