Information on EC 3.6.1.57 - UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose hydrolase

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The expected taxonomic range for this enzyme is: Campylobacter jejuni

EC NUMBER
COMMENTARY hide
3.6.1.57
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RECOMMENDED NAME
GeneOntology No.
UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
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Biosynthesis of antibiotics
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CMP-pseudaminate biosynthesis
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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
?
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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 SUBSTRATES
NATURAL PRODUCTS
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
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this enzyme is independent of the presence of divalent metal ions
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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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
5444
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
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assay at
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32380
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His6-tagged enzyme, electrospray ionization mass spectrometry
32383
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1 * 32383, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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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.
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant enzymes
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H17F
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almost complete inactivation
H17L
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almost complete inactivation
H17N
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kcat/KM for UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose is 9.4% of the wild-type value
N255A
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kcat/KM for UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose is 0.64% of the wild-type value
Y78F
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kcat/KM for UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose is 2.1% of the wild-type value