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Information on EC 3.6.1.57 - UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose hydrolase and Organism(s) Campylobacter jejuni and UniProt Accession Q0P8U5

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IUBMB Comments
The enzyme is involved in biosynthesis of pseudaminic acid.
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This record set is specific for:
Campylobacter jejuni
UNIPROT: Q0P8U5
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The taxonomic range for the selected organisms is: Campylobacter jejuni
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
udp-6-deoxy-altdinac hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
UDP-6-deoxy-AltdiNAc hydrolase
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SYSTEMATIC NAME
IUBMB Comments
UDP-2,4-bis(acetamido)-2,4,6-trideoxy-beta-L-altropyranose hydrolase
The enzyme is involved in biosynthesis of pseudaminic acid.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose + H2O
2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose + UDP
show the reaction diagram
additional information
?
-
molecular modeling identifies a His17-coordinated water molecule as the putative nucleophile and suggests the UDP-sugar substrate adopts a twist-boat conformation upon binding to PseG, enhancing the exposure of the anomeric bond cleaved and favoring inversion at C1
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-
?
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
UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose + H2O
2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose + UDP
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
weak inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.174 - 1.3
UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.27 - 26.6
UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6 - 152.9
UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32380
His6-tagged enzyme, electrospray ionization mass spectrometry
32383
1 * 32383, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 32383, calculated from sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of Campylobacter jejuni PseG in apo-form and as a complex with its UDP product at 1.8 and 1.85 A resolution.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H17F
almost complete inactivation
H17L
almost complete inactivation
H17N
kcat/KM for UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose is 9.4% of the wild-type value
N255A
kcat/KM for UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose is 0.64% of the wild-type value
Y78F
kcat/KM for UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose is 2.1% of the wild-type value
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant enzymes
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liu, F.; Tanner, M.E.
PseG of pseudaminic acid biosynthesis: a UDP-sugar hydrolase as a masked glycosyltransferase
J. Biol. Chem.
281
20902-20909
2006
Campylobacter jejuni (Q0P8U5), Campylobacter jejuni
Manually annotated by BRENDA team
Rangarajan, E.S.; Proteau, A.; Cui, Q.; Logan, S.M.; Potetinova, Z.; Whitfield, D.; Purisima, E.O.; Cygler, M.; Matte, A.; Sulea, T.; Schoenhofen, I.C.
Structural and functional analysis of Campylobacter jejuni PseG: a udp-sugar hydrolase from the pseudaminic acid biosynthetic pathway
J. Biol. Chem.
284
20989-21000
2009
Campylobacter jejuni (Q0P8U5)
Manually annotated by BRENDA team