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Information on EC 5.4.99.62 - D-ribose pyranase and Organism(s) Escherichia coli and UniProt Accession P04982

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     5 Isomerases
         5.4 Intramolecular transferases
             5.4.99 Transferring other groups
                5.4.99.62 D-ribose pyranase
IUBMB Comments
The enzyme also catalyses the conversion between beta-allopyranose and beta-allofuranose.
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This record set is specific for:
Escherichia coli
UNIPROT: P04982
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
d-ribose pyranase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
D-ribopyranose furanomutase
The enzyme also catalyses the conversion between beta-allopyranose and beta-allofuranose.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-allopyranose
beta-allofuranose
show the reaction diagram
-
-
-
?
beta-D-ribopyranose
beta-D-ribofuranose
show the reaction diagram
-
-
-
?
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
beta-D-ribopyranose
beta-D-ribofuranose
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the level of pyranase rbsD transcription increases markedly in a LacI-type transcription factor RbsR knockout mutant. In the presence of D-ribose, the level of rbsD mRNA in wild-type significantly increases but it does not show any change in the rbsR mutant
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
10 * 14000, SDS-PAGE, main form plus apparently larger oligomeric forms
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
10 * 14000, SDS-PAGE, main form plus apparently larger oligomeric forms
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.9 A resolution. Protein forms a decameric toroid with each active site formed by two adjacent subunits. While one subunit provides most of the fucose-interacting residues including a catalytic tyrosine residue, the other subunit provides a catalytic His-Asp dyad. This active-site feature is critical both for the mutarotase activity toward L-fucose and for the pyranase activity toward D-ribose
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H106A
the mutant enzyme retains one-third of the original pyranase activity, the mutant proteins are able to form an oligomer as is the case for the wild type, mutant binds to ribose as much as the wild type does,
H20A
mutation completely abolishes the pyranase activity, the mutant proteins are able to form an oligomer as is the case for the wild type, mutant binds to ribose as much as the wild type does,
D64N
mutant exhibits significantly reduced catalytic activity toward D-ribose
H22A
mutant exhibits significantly reduced catalytic activity toward D-ribose
Y111F
mutant exhibits significantly reduced catalytic activity toward D-ribose
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the level of pyranase rbsD transcription increases markedly in a LacI-type transcription factor RbsR knockout mutant. In the presence of D-ribose, the level of rbsD mRNA in wild-type significantly increases but it does not show any change in the rbsR mutant
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
after being completely denatured in the presence of 8 M urea, isoform RbsD is able to refold and reassemble spontaneously. The oligomeric size of the protein appears to be fully recovered. Urea-induced disassembly occurs in a stepwise manner. The disassembly intermediates lose almost all their secondary structures. Reassembly of RbsD is a fast and apparently nonstepwise process
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ryu, K.S.; Kim, C.; Kim, I.; Yoo, S.; Choi, B.S.; Park, C.
NMR application probes a novel and ubiquitous family of enzymes that alter monosaccharide configuration
J. Biol. Chem.
279
25544-25548
2004
Escherichia coli (P04982)
Manually annotated by BRENDA team
Lee, K.H.; Ryu, K.S.; Kim, M.S.; Suh, H.Y.; Ku, B.; Song, Y.L.; Ko, S.; Lee, W., Oh, B.H.
Crystal structures and enzyme mechanisms of a dual fucose mutarotase/ribose pyranase
J. Mol. Biol.
391
178-191
2009
Escherichia coli (P0AEN8), Mus musculus (Q8R2K1)
Manually annotated by BRENDA team
Shimada, T.; Kori, A.; Ishihama, A.
Involvement of the ribose operon repressor RbsR in regulation of purine nucleotide synthesis in Escherichia coli
FEMS Microbiol. Lett.
344
159-165
2013
Escherichia coli
Manually annotated by BRENDA team
Feng, Y.; Jiao, W.; Fu, X.; Chang, Z.
Stepwise disassembly and apparent nonstepwise reassembly for the oligomeric RbsD protein
Protein Sci.
15
1441-1448
2006
Escherichia coli (P04982)
Manually annotated by BRENDA team