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Enzyme Nomenclature
Information on EC 4.1.3.3 - N-acetylneuraminate lyase
for references in articles please use BRENDA:EC4.1.3.3
Word Map on EC 4.1.3.3
- 4.1.3.3
- mannac
-
2-epimerase
- n-acetylmannosamine
-
aldolases
- dihydrodipicolinate
-
n-glycolylneuraminic
-
cmp-sialic
-
3.2.1.18
- dhdps
- synthesis
- n-acylneuraminate
- neu5gc
- biotechnology
- analysis
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
4.1.3.3
-
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RECOMMENDED NAME
GeneOntology No.
N-acetylneuraminate lyase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-acetylneuraminate = N-acetyl-D-mannosamine + pyruvate
mechanism
-
N-acetylneuraminate = N-acetyl-D-mannosamine + pyruvate
mechanism
-
N-acetylneuraminate = N-acetyl-D-mannosamine + pyruvate
the enzyme catalyzes a Bi-Uni ordered condensation reaction in which pyruvate binds first to the enzyme to form a catalytically important Schiff base. Tyr137 acts as the proton donor to the aldehyde oxygen of ManNAc during the reaction, the activation barrier is dominated by carbon-carbon bond formation, and proton transfer from Tyr137 is required to obtain a stable Neu5Ac-Lys165 Schiff base complex. A triad of residues, Tyr137, Ser47, and Tyr110 from a neighboring subunit, are required to correctly position Tyr137 for its function
-
N-acetylneuraminate = N-acetyl-D-mannosamine + pyruvate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-C-bond cleavage
condensation
-
-
-
-
elimination
-
-
of an oxo-acid, C-C bond cleavage
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
N-acetylneuraminate pyruvate-lyase (N-acetyl-D-mannosamine-forming)
Also acts on N-glycoloylneuraminate, and on O-acetylated sialic acids, other than 4-O-acetylated derivatives.
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CAS REGISTRY NUMBER
COMMENTARY
9027-60-5
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
subspecies aureus, methicillin-resistant, gene nanA
UniProt
-
33314, 33322, 33323, 33324, 33330, 33331, 33332, 33333, 33334, 33335, 33336, 650772, 658576, 666750, 666805, 674987, 677556, 678004, 682230, 682313, 701855, 701881, 713852, 715921, 727186
-
-
the sequence of the cloned gene differs on six bases, T228C, T303C, C624T, G777A, C786T and C832T
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
-
reaction mechanism by crystal structure analysis, and quantum mechanical/molecular mechanical modeling, overview
physiological function
-
the quaternary structure of Escherichia coli N-acetylneuraminate lyase is essential for functional expression
physiological function
-
the enzyme regulates the cellular concentrations of sialic acid and preventing the recycling of sialic acid for further sialiation with glycoconjuates in the Golgi compartment. The enzyme plays a dispensable role in uterine function and embryo development
physiological function
Escherichia coli W3110 / ATCC 27325
-
the quaternary structure of Escherichia coli N-acetylneuraminate lyase is essential for functional expression
-
physiological function
-
the enzyme regulates the cellular concentrations of sialic acid and preventing the recycling of sialic acid for further sialiation with glycoconjuates in the Golgi compartment. The enzyme plays a dispensable role in uterine function and embryo development
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid
?
-
-
-
-
?
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
pyruvate + (2R,3S)-2,3-dihydroxy-4-oxo-N,N-dipropylbutanamide
-
-
-
-
r
2-deoxy-2-[[(alpha-D-galactopyranosyloxy)acetyl]amino]-D-mannopyranose + pyruvate
3,5-dideoxy-5-[[(alpha-D-galactopyranosyloxy)acetyl]amino]-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
-
-
36% yield
-
?
2-deoxy-2-[[(beta-D-galactopyranosyloxy)acetyl]amino]-D-mannopyranose + pyruvate
3,5-dideoxy-5-[[(beta-D-galactopyranosyloxy)acetyl]amino]-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
-
-
34% yield
-
?
3-bromo-3-deoxy-D-mannose + pyruvate
?
-
wild-type enzyme: 5% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I: 5% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I/V265I: 10% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C: 10% of the activity with N-acetyl-D-mannosamine, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y: 10% of the activity with N-acetyl-D-mannosamine
-
-
?
4-O-alpha-D-galactopyranosyl-D-mannopyranose + pyruvate
3-deoxy-7-O-alpha-D-galactopyranosyl-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
-
-
5% yield
-
?
4-O-beta-D-galactopyranosyl-D-mannopyranose + pyruvate
3-deoxy-7-O-beta-D-galactopyranosyl-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
-
-
38% yield
-
?
4-O-beta-D-glucopyranosyl-D-mannopyranose + pyruvate
3-deoxy-7-O-beta-D-glucopyranosyl-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
-
-
35% yield
-
?
5-N-acetyl-4-O-acetylneuraminic acid
?
-
22% the activity with N-acetylneuraminic acid
-
?
5-O-alpha-D-galactopyranosyl-alpha-D-mannofuranose + pyruvate
3-deoxy-8-O-alpha-D-galactopyranosyl-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
-
-
62% yield
-
?
5-O-beta-D-galactopyranosyl-alpha-D-mannofuranose + pyruvate
3-deoxy-8-O-beta-D-galactopyranosyl-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
-
-
85% yield
-
?
5-O-methyl-N-acetyl-D-mannosamine + pyruvate
8-O-methyl-N-acetylneuraminate
-
-
-
-
6-O-alpha-D-galactopyranosyl-D-mannopyranose + pyruvate
3-deoxy-9-O-alpha-D-galactopyranosyl-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
-
-
81% yield
-
?
6-O-alpha-D-glucopyranosyl-D-mannopyranose + pyruvate
3-deoxy-9-O-alpha-D-glucopyranosyl-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
-
-
65% yield
-
?
6-O-alpha-D-mannopyranosyl-D-mannopyranose + pyruvate
3-deoxy-9-O-alpha-D-mannopyranosyl-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
-
-
78% yield
-
?
6-O-beta-D-glucopyranosyl-D-mannopyranose + pyruvate
3-deoxy-9-O-beta-D-glucopyranosyl-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
-
-
83% yield
-
?
D-arabinose + pyruvate
D-3-deoxy-manno-2-octulosonic acid
-
wild-type enzyme: 20% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I: 40% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I/V265I: 65% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C: 40% of the activity with N-acetyl-D-mannosamine, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y: 85% of the activity with N-acetyl-D-mannosamine
-
-
r
D-glucose + pyruvate
?
-
wild-type enzyme: 40% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I: 40% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I/V265I: 20% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C: 25% of the activity with N-acetyl-D-mannosamine, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y: 20% of the activity with N-acetyl-D-mannosamine
-
-
?
D-gulose + pyruvate
?
-
wild-type enzyme: 10% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I/V265I: 110% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C: 90% of the activity with N-acetyl-D-mannosamine, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y: 70% of the activity with N-acetyl-D-mannosamine
-
-
?
D-mannosamine + pyruvate
?
-
wild-type enzyme: 80% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I: 90% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I/V265I: 165% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C: 190% of the activity with N-acetyl-D-mannosamine, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y: 170% of the activity with N-acetyl-D-mannosamine
-
-
?
D-mannose + pyruvate
?
-
wild-type enzyme: 30% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I: 15% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I/V265I: 70% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C: 80% of the activity with N-acetyl-D-mannosamine, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y: 75% of the activity with N-acetyl-D-mannosamine
-
-
?
D-mannose + pyruvic acid
2-keto-3-deoxy-D-glycero-D-galacto-nonopyranulosonic acid
-
-
-
-
?
D-talose + pyruvate
?
-
wild-type enzyme: 60% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I: 50% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I/V265I: 105% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C: 80% of the activity with N-acetyl-D-mannosamine, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y: 70% of the activity with N-acetyl-D-mannosamine
-
-
?
D-xylose + pyruvate
?
-
wild-type enzyme: 45% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I: 40% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I/V265I: 55% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C: 25% of the activity with N-acetyl-D-mannosamine, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y: 25% of the activity with N-acetyl-D-mannosamine
-
-
?
L-arabinose + pyruvate
L-3-deoxy-manno-2-octulosonic acid
-
wild-type enzyme: 10% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I: 35% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I/V265I: 70% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C: 40% of the activity with N-acetyl-D-mannosamine, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y: 80% of the activity with N-acetyl-D-mannosamine
-
-
r
L-gulose + pyruvate
?
-
wild-type enzyme: 70% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I: 35% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I/V265I: 15% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C: 15% of the activity with N-acetyl-D-mannosamine, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y: 15% of the activity with N-acetyl-D-mannosamine
-
-
?
L-mannose + pyruvate
?
-
wild-type enzyme: 80% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I: 110% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I/V265I: 95% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C: 95% of the activity with N-acetyl-D-mannosamine, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y: 95% of the activity with N-acetyl-D-mannosamine
-
-
?
N-acetyl-D-mannosamine + pyruvate
N-acetyl-D-neuraminic acid
-
-
-
-
r
N-acetyl-L-mannosamine + pyruvate
N-acetyl-L-neuraminic acid
-
wild-type enzyme: 0.2% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I: 0.5% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/V251I/V265I: 1% of the activity with N-acetyl-D-mannosamine, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C: 2% of the activity with N-acetyl-D-mannosamine, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y: 2% of the activity with N-acetyl-D-mannosamine
-
-
r
pyruvate + alpha-D-Galp-(1,6)-D-Manp
alpha-D-Galp-(1,9)-D-deoxyneuraminic acid
-
-
-
-
?
5-N-acetyl-9-O-acetylneuraminic acid
?
-
54% the activity with N-acetylneuraminic acid
-
?
5-N-acetyl-9-O-acetylneuraminic acid
?
-
32.45% the activity with N-acetylneuraminic acid
-
?
5-N-acetyl-9-O-acetylneuraminic acid
?
-
45% the activity with N-acetylneuraminic acid
-
?
N-acetyl-D-mannosamine + pyruvate
N-acetylneuraminate
the enzyme catalyzes the retro-aldol cleavage of N-acetylneuraminic acid to form N-acetyl-D-mannosamine and pyruvate
-
-
r
N-acetyl-D-mannosamine + pyruvate
N-acetylneuraminate
the enzyme catalyzes the retro-aldol cleavage of N-acetylneuraminic acid to form N-acetyl-D-mannosamine and pyruvate
-
-
r
N-acetyl-D-mannosamine + pyruvate
N-acetylneuraminate
reversible aldol condensation of pyruvate and N-acetyl-D-mannosamine
-
-
r
N-acetyl-D-mannosamine + pyruvate
N-acetylneuraminate
reversible aldol condensation of pyruvate and N-acetyl-D-mannosamine
-
-
r
N-Acetyl-D-mannosamine + pyruvate
N-Acetylneuraminic acid
-
-
-
r
N-Acetyl-D-mannosamine + pyruvate
N-Acetylneuraminic acid
-
-
-
r
N-acetyl-D-neuraminic acid
N-acetyl-D-mannosamine + pyruvate
-
in presence of excess pyruvate the equilibrium may be driven in the direction of aldol product formation
-
-
r
N-acetyl-D-neuraminic acid
N-acetyl-D-mannosamine + pyruvate
-
-
-
-
r
N-acetyl-D-neuraminic acid
pyruvate + N-acetyl-D-mannosamine
-
-
-
-
r
N-acetyl-D-neuraminic acid
pyruvate + N-acetyl-D-mannosamine
-
-
-
-
r
N-acetyl-neuraminic acid
N-acetyl-D-mannosamine + pyruvate
-
-
-
-
r
N-Acetylmannosamine + pyruvate
?
-
N-acetylneuraminic acid is intermediate for colomic acid biosynthesis
-
-
-
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
-
-
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
-
the enzyme catalyzes the reversible condensation of pyruvate with N-acetyl-D-mannosamine to yield the sialic acid N-acetylneuraminic acid
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
K0Y2E6
reversible aldol cleavage of N-acetylneuraminic acid
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
-
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
-
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
-
-
-
r
N-Acetylneuraminic acid
?
Corynebacterium belfanti
-
metabolized by pathogens parasitizing on mucous membranes
-
-
-
N-Acetylneuraminic acid
?
-
metabolized by pathogens parasitizing on mucous membranes
-
-
-
N-Acetylneuraminic acid
?
-
metabolized by pathogens parasitizing on mucous membranes
-
-
-
N-Acetylneuraminic acid
?
-
metabolized by pathogens parasitizing on mucous membranes
-
-
-
N-Acetylneuraminic acid
?
-
N-acetylneuraminate lyase plays important role in regulation of N-acetylneuraminic acid metabolism
-
-
-
N-Acetylneuraminic acid
?
-
metabolized by pathogens parasitizing on mucous membranes
-
-
-
N-Acetylneuraminic acid
N-Acetyl-D-mannosamine + pyruvate
-
-
-
-
-
N-Acetylneuraminic acid
N-Acetyl-D-mannosamine + pyruvate
-
-
-
-
r
N-Acetylneuraminic acid
N-Acetyl-D-mannosamine + pyruvate
-
-
-
r
N-Acetylneuraminic acid
N-Acetyl-D-mannosamine + pyruvate
-
-
-
r
N-Acetylneuraminic acid
N-Acetyl-D-mannosamine + pyruvate
-
-
-
r
N-Acetylneuraminic acid
N-Acetyl-D-mannosamine + pyruvate
-
-
-
-
?
N-Acetylneuraminic acid
N-Acetyl-D-mannosamine + pyruvate
-
-
-
-
?
N-Acetylneuraminic acid
N-Acetyl-D-mannosamine + pyruvate
-
-
r
N-Acetylneuraminic acid
N-Acetyl-D-mannosamine + pyruvate
-
syn: Neu5Ac
-
r
N-Acetylneuraminic acid
N-Acetyl-D-mannosamine + pyruvate
-
-
-
-
-
N-Acetylneuraminic acid
N-Acetyl-D-mannosamine + pyruvate
-
-
-
r
N-Acetylneuraminic acid
N-Acetyl-D-mannosamine + pyruvate
-
formation of a Schiff base
-
r
N-Acetylneuraminic acid
N-Acetyl-D-mannosamine + pyruvate
-
regulation of sialic acid metabolism
-
r
N-Glycolylneuraminic acid
?
-
60% the rate of N-acetylneuraminic acid
-
?
N-Glycolylneuraminic acid
?
-
47% the activity with N-acetylneuraminic acid
-
?
additional information
?
-
-
structural characteristics of substrates
-
-
-
additional information
?
-
-
configuration of substrate and products
-
-
-
additional information
?
-
-
condensation: N-acetylglucosamine, N-acetylgalactosamine, glucosamine and galactosamine cannot replace N-acetylmannosamine. Phosphoenolpyruvate, lactate, beta-hydroxypyruvate and other pyruvate derivatives cannot replace pyruvate
-
-
-
additional information
?
-
-
no substrates are 3-azido-3-deoxy, 3-amino-3-deoxy and 3-N-tert-butylcarbonyl-3-deoxy derivatives of 2-acetamido-2-deoxy-alpha,beta-D-mannose
-
?
additional information
?
-
-
One point mutation (L142R) is sufficient to create an enzyme that can complement a bacterial auxotroph lacking the gene for dihydrodipicolinate synthase, EC 4.2.1.52. The mutant enzyme catalyzes the reaction: L-aspartate 4-semialdehyde + pyruvate = dihydrodipicolinate + 2 H2O
-
?
additional information
?
-
-
not: N-acetyl-4-O-acetylneuraminic acid and 2-deoxy-2,3-didehydro-N-acetylneuraminic acid
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-Acetylneuraminic acid
N-Acetyl-D-mannosamine + pyruvate
-
regulation of sialic acid metabolism
-
r
N-acetyl-D-mannosamine + pyruvate
N-acetylneuraminate
Q6GK01
the enzyme catalyzes the retro-aldol cleavage of N-acetylneuraminic acid to form N-acetyl-D-mannosamine and pyruvate
-
-
r
N-acetyl-D-mannosamine + pyruvate
N-acetylneuraminate
Q6GK01
the enzyme catalyzes the retro-aldol cleavage of N-acetylneuraminic acid to form N-acetyl-D-mannosamine and pyruvate
-
-
r
N-acetyl-D-mannosamine + pyruvate
N-acetylneuraminate
B9DIJ2
reversible aldol condensation of pyruvate and N-acetyl-D-mannosamine
-
-
r
N-acetyl-D-mannosamine + pyruvate
N-acetylneuraminate
B9DIJ2
reversible aldol condensation of pyruvate and N-acetyl-D-mannosamine
-
-
r
N-Acetylmannosamine + pyruvate
?
-
N-acetylneuraminic acid is intermediate for colomic acid biosynthesis
-
-
-
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
Q2G160
-
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
B9DIJ2
-
-
-
r
N-Acetylneuraminic acid
?
Corynebacterium belfanti
-
metabolized by pathogens parasitizing on mucous membranes
-
-
-
N-Acetylneuraminic acid
?
-
metabolized by pathogens parasitizing on mucous membranes
-
-
-
N-Acetylneuraminic acid
?
-
metabolized by pathogens parasitizing on mucous membranes
-
-
-
N-Acetylneuraminic acid
?
-
metabolized by pathogens parasitizing on mucous membranes
-
-
-
N-Acetylneuraminic acid
?
-
N-acetylneuraminate lyase plays important role in regulation of N-acetylneuraminic acid metabolism
-
-
-
N-Acetylneuraminic acid
?
-
metabolized by pathogens parasitizing on mucous membranes
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hydrogen peroxide
-
0% residual activity at 10 mM, 16% residual activity at 1 mM
L-lysine
-
50% inhibition at 0.2 mM, inhibits wild-type enzyme, but not mutant enzymes
Bromopyruvate
-
50% residual activity after incubation for 4.2 min with 1 mM bromopyruvate at pH 7.2, 37°C
N-bromosuccinimide
-
0% residual activity at 0.01 mM, 36% residual activity at 0.001 mM
N-bromosuccinimide
-
0% residual activity at 0.1 mM, 36% residual activity at 0.01 mM
p-chloromercuribenzoate
-
0% residual activity at 0.1 mM, 9% residual activity at 0.01 mM
p-chloromercuribenzoate
-
0% residual activity at 0.01 mM, 44% residual activity at 0.001 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.39 - 11
(2R,3R,4R)-6-[(aminooxy)carbonyl]-3,4,6-trihydroxy-N-propyltetrahydro-2H-pyran-2-carboxamide
0.35 - 10.6
(2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid
additional information
additional information
-
with substrate N-acetylneuraminic acid increasing Km with increasing pH
-
0.39
(2R,3R,4R)-6-[(aminooxy)carbonyl]-3,4,6-trihydroxy-N-propyltetrahydro-2H-pyran-2-carboxamide
-
mutant enzyme E192N
11
(2R,3R,4R)-6-[(aminooxy)carbonyl]-3,4,6-trihydroxy-N-propyltetrahydro-2H-pyran-2-carboxamide
-
wild-type enzyme
0.35
(2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid
-
pH 7.5, 25°C, mutant enzyme E192V
0.39
(2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid
-
pH 7.5, 25°C, mutant enzyme E192N
0.5
(2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid
-
pH 7.5, 25°C, mutant enzyme E192S
2.54
(2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid
-
pH 7.5, 25°C, mutant enzyme S208G
5.7
(2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid
-
pH 7.5, 25°C, mutant enzyme D191P
10.6
(2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid
-
pH 7.5, 25°C, wild-type enzyme
0.2
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192M mutant protein, pH 7.5, 25°C; E192P mutant protein, pH 7.5, 25°C
0.3
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192F mutant protein, pH 7.5, 25°C
0.4
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192N mutant protein, pH 7.7.5, 25°C; E192V mutant protein, pH 7.5, 25°C
0.5
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192H mutant protein, pH 7.5, 25°C
0.6
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192S mutant protein, pH 7.5, 25°C
0.7
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192Q mutant protein, pH 7.5, 25°C
1.1
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192D mutant protein, pH 7.5, 25°C
11
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
wild type (E192), pH 7.5, 25°C
3.5
D-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/V251I/V265I
6.3
D-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C
11.4
D-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y
12.3
D-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L
14.5
D-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/V251I
2.4
L-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C
2.7
L-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/V251I/V265I
2.8
L-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y
9.2
L-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/V251I
14.1
L-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L
131.7
N-acetyl-D-mannosamine
-
recombinant enzyme, pH and temperature not specified in the publication
149
N-acetyl-D-mannosamine
recombinant His-taggged enzyme, pH 7.0, 37°C
160
N-acetyl-D-mannosamine
-
soluble enzyme, pH not specified in the publication, temperature not specified in the publication
245
N-acetyl-D-mannosamine
-
cross-linked enzyme aggregates, pH 7.5, 37°C
3.9
N-acetyl-D-neuraminic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/V251I
10.1
N-acetyl-D-neuraminic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C
12.1
N-acetyl-D-neuraminic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/V251I/V265I
15.3
N-acetyl-D-neuraminic acid
-
pH 7.5, 25°C, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y
3 - 3.5
N-acetyl-L-neuraminic acid
-
pH 7.5, 25°C, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y
36.2
N-acetyl-L-neuraminic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C
127
N-acetyl-L-neuraminic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/V251I/V265I
369.4
N-acetyl-L-neuraminic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/V251I
0.013
N-acetylneuraminate
purified recombinant mutant K165C, pH 7.4, 30°C
0.015
N-acetylneuraminate
purified recombinant mutant K165-gamma-thialysine, pH 6.8, 30°C
0.023
N-acetylneuraminate
purified recombinant mutant K165-gamma-thialysine, pH 7.4, 30°C
0.036
N-acetylneuraminate
purified recombinant wild-type enzyme, pH 7.4, 30°C
0.04
N-acetylneuraminate
purified recombinant wild-type enzyme, pH 6.8, 30°C
2
N-acetylneuraminate
recombinant His-taggged enzyme, pH 7.0, 37°C
2.51
N-acetylneuraminate
-
mutant enzyme L171N/I229N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
3.2
N-acetylneuraminate
-
mutant enzyme L199N/I229D, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
3.4
N-acetylneuraminate
-
mutant enzyme I229N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
3.42
N-acetylneuraminate
-
mutant enzyme L171R, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
3.93
N-acetylneuraminate
-
mutant enzyme I229R, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
4
N-acetylneuraminate
-
mutant enzyme L199N/I229R, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
4
N-acetylneuraminate
-
recombinant enzyme, pH and temperature not specified in the publication
4.1
N-acetylneuraminate
-
wild type enzyme, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
4.3
N-acetylneuraminate
-
mutant enzyme L199N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
4.7
N-acetylneuraminate
-
mutant enzyme L199N/I229N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
5
N-acetylneuraminate
-
mutant enzyme I229D, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
6.1
N-acetylneuraminate
-
mutant enzyme L199R/I229N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
2
N-acetylneuraminic acid
-
pH 7.2, 50 mM phosphate buffer, wild-type
3.2
N-acetylneuraminic acid
-
pH 7.2, 250 mM phosphate buffer, wild-type
6
N-acetylneuraminic acid
-
E192P mutant protein, pH 7.5, 25°C; E192S mutant protein, pH 7.5, 25°C
19.9
pyruvate
-
soluble enzyme, pH not specified in the publication, temperature not specified in the publication
35.1
pyruvate
-
recombinant enzyme, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.057 - 10.83
(2R,3R,4R)-6-[(aminooxy)carbonyl]-3,4,6-trihydroxy-N-propyltetrahydro-2H-pyran-2-carboxamide
0.44 - 2.18
(2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid
0.057 - 0.65
(2R,3R,4R)-6-[(aminooxy)carbonyl]-3,4,6-trihydroxy-N-propyltetrahydro-2H-pyran-2-carboxamide
-
mutant enzyme E192N
1.23
(2R,3R,4R)-6-[(aminooxy)carbonyl]-3,4,6-trihydroxy-N-propyltetrahydro-2H-pyran-2-carboxamide
-
wild-type enzyme
10.83
(2R,3R,4R)-6-[(aminooxy)carbonyl]-3,4,6-trihydroxy-N-propyltetrahydro-2H-pyran-2-carboxamide
-
mutant enzyme E192N
0.44
(2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid
-
pH 7.5, 25°C, mutant enzyme S208G
0.91
(2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid
-
pH 7.5, 25°C, mutant enzyme D191P
1.22
(2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid
-
pH 7.5, 25°C, wild-type enzyme
1.58
(2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid
-
pH 7.5, 25°C, mutant enzyme E192V
1.85
(2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid
-
pH 7.5, 25°C, mutant enzyme E192S
2.18
(2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid
-
pH 7.5, 25°C, mutant enzyme E192N
0.1
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192D mutant protein, pH 7.5, 25°C
0.43
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192S mutant protein, pH 7.5, 25°C
0.63
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192H mutant protein, pH 7.5, 25°C
0.82
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192P mutant protein, pH 7.5, 25°C
1.17
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192M mutant protein, pH 7.5, 25°C
1.22
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
wild type (E192), pH 7.5, 25°C
1.47
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192F mutant protein, pH 7.5, 25°C
1.58
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192V mutant protein, pH 7.5, 25°C
2.17
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192N mutant protein, pH 7.7.5, 25°C
2.83
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192Q mutant protein, pH 7.5, 25°C
1.5
D-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L
2.8
D-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/V251I
3.2
D-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/V251I/V265I
5.1
D-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C
8.9
D-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y
1.1
L-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L; pH 7.5, 25°C, wild-type enzyme
1.9
L-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/V251I
2.5
L-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/V251I/V265I
4.2
L-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C
10.4
L-3-deoxy-manno-2-octulosonic acid
-
pH 7.5, 25°C, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y
4.5
N-acetyl-D-mannosamine
recombinant His-taggged enzyme, pH 7.0, 37°C
1.5
N-acetyl-D-neuraminic acid
-
pH 7.5, 25°C, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y
1.7
N-acetyl-D-neuraminic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C
2.2
N-acetyl-D-neuraminic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/V251I/V265I
9.7
N-acetyl-D-neuraminic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/V251I
0.0045
N-acetyl-L-neuraminic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/V251I
0.0068
N-acetyl-L-neuraminic acid
-
pH 7.5, 25°C, mutant enzyme Y98H/F115L/V251I/V265I
0.02
N-acetyl-L-neuraminic acid
-
pH 7.5, 25°C, mutant enzyme E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y; pH 7.5, 25°C, mutant enzyme Y98H/F115L/N153Y/V251I/V265I/Y281C
0.013
N-acetylneuraminate
purified recombinant mutant K165C, pH 7.4, 30°C
0.015
N-acetylneuraminate
purified recombinant mutant K165-gamma-thialysine, pH 6.8, 30°C
0.023
N-acetylneuraminate
purified recombinant mutant K165-gamma-thialysine, pH 7.4, 30°C
0.036
N-acetylneuraminate
purified recombinant wild-type enzyme, pH 7.4, 30°C
0.04
N-acetylneuraminate
purified recombinant wild-type enzyme, pH 6.8, 30°C
0.29
N-acetylneuraminate
-
mutant enzyme L199N/I229D, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
0.664
N-acetylneuraminate
-
mutant enzyme L199N/I229N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
3.15
N-acetylneuraminate
-
mutant enzyme L171N/I229N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
4
N-acetylneuraminate
recombinant His-taggged enzyme, pH 7.0, 37°C
4.69
N-acetylneuraminate
-
mutant enzyme I229D, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
5.49
N-acetylneuraminate
-
mutant enzyme L171R, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
6.75
N-acetylneuraminate
-
wild type enzyme, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
7.4
N-acetylneuraminate
-
mutant enzyme I229N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
7.72
N-acetylneuraminate
-
mutant enzyme I229R, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
7.94
N-acetylneuraminate
-
mutant enzyme L199N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
8.9
N-acetylneuraminate
-
mutant enzyme L199N/I229R, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
11.87
N-acetylneuraminate
-
mutant enzyme L199R/I229N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
2
N-acetylneuraminic acid
-
E192D mutant protein, pH 7.5, 25°C; E192H mutant protein, pH 7.5, 25°C; E192V mutant protein, pH 7.5, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192D mutant protein, pH 7.5, 25°C
0.12
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
wild type (E192), pH 7.5, 25°C
0.7
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192S mutant protein, pH 7.5, 25°C
1.33
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192H mutant protein, pH 7.5, 25°C
4.17
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192Q mutant protein, pH 7.5, 25°C
4.33
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192P mutant protein, pH 7.5, 25°C
4.5
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192V mutant protein, pH 7.5, 25°C
5.17
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192F mutant protein, pH 7.5, 25°C
5.33
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192M mutant protein, pH 7.5, 25°C
5.67
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
E192N mutant protein, pH 7.7.5, 25°C
0.0074
N-acetyl-D-mannosamine
-
cross-linked enzyme aggregates, pH 7.5, 37°C
0.03
N-acetyl-D-mannosamine
-
soluble enzyme, pH not specified in the publication, temperature not specified in the publication
0.03
N-acetyl-D-mannosamine
recombinant His-taggged enzyme, pH 7.0, 37°C
0.08
N-acetyl-D-mannosamine
-
recombinant enzyme, pH and temperature not specified in the publication
1.9
N-acetylneuraminate
-
recombinant enzyme, pH and temperature not specified in the publication
2
N-acetylneuraminate
recombinant His-taggged enzyme, pH 7.0, 37°C
0.07
N-acetylneuraminic acid
-
E192N mutant protein, pH 7.7.5, 25°C; E192P mutant protein, pH 7.5, 25°C
0.08
pyruvate
-
recombinant enzyme, pH and temperature not specified in the publication
0.11
pyruvate
-
soluble enzyme, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3
(2R,3R)-2,3,4-trihydroxy-N,N-dipropylbutanamide
-
E192N mutant protein , pH 7.5, 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0693
immobilized recombinant enzyme, the activity yield of immobilized enzyme is approximately 10% of the free enzyme
10
11
purified recombinant enzyme, pH 8.0, temperature not specified in the publication
36.26
additional information
36.26
-
after 14.8fold purification, in 50 mM potassium phosphate buffer, pH 7.5, at 37°C
36.26
purified enzyme after expression in Escherichia coli cells, enzyme activity is assayed in reaction solution (20 mM N-acetyl-D-neuraminic acid in 50 mM potassium phosphate buffer, pH 7.5)
additional information
-
after a 36 h incubation, the concentrations of N-acetyl-D-neuraminic acid from the reactions utilizing 0.4, 0.8, 1.2, 1.6, 2.0, and 2.2 M pyruvate as the carbon source are 7.5 (3.75%), 26.9 (3.45%), 43.9 (21.95%), 56.0 (28%), and 61.9 mM (30.95%), respectively. When using 2.2 M pyruvate, in the first 6 h, the concentration of N-acetyl-D-neuraminic acid reaches 29.5 mM (which is about half of the maximal concentration), and the productivity of N-acetyl-D-neuraminic acid is 1.6 g/l/h, the concentration of the intermediate N-acetyl-D-mannosamine also increases gradually from 0 to 64 mM during the process
additional information
cell density of Escherichia coli BL21 (DE3) carrying the pNA1 plasmid is 37 (OD600) after fermentation for 15 h, and the highest activity for N-acetyl-D-neuraminic acid lyase is 8.472 U/ml after fermentation for 9 h, enzyme activity is assayed in reaction solution (20 mM Neu5Ac in 50 mM potassium phosphate buffer, pH 7.5)
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7
7.2
7.4
7.5
7.5
7.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
6 - 9
6 - 9
pH-activity profiles of the K165-gamma-thialysine mutant enzyme, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
50
60
70
75
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 80
synthesis and hydrolysis reactions, profiles, overview
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
progesterone-mediated dynamic expression of the enzyme in the periimplantation uterus, Npl expression increases 56fold from gestation day 0.5 to day 2.5. In ovariectomized mouse uterus
-
progesterone-mediated dynamic expression of the enzyme in the periimplantation uterus, Npl expression increases 56fold from gestation day 0.5 to day 2.5. In ovariectomized mouse uterus
-
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
33700
33992
x * 33992, recombinant His6-tagged wild-type enzyme, mass spectrometry
35000
55000
100000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
tetramer
trimer
?
x * 33992, recombinant His6-tagged wild-type enzyme, mass spectrometry
?
-
x * 33992, recombinant His6-tagged wild-type enzyme, mass spectrometry
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L142R mutant, complexed with beta-hydroxypyruvate, hanging drop vapor diffusion method
-
mutant enzyme E192N, in complex with pyruvate, sitting drop vapor diffusion method, using 100 mM Tris-HCl pH 8.2, 200 mM ammonium acetate, 18% PEG 3350
-
complexed with sialic acid alditol, 4-deoxy-sialic acid or 4-oxo-sialic acid, microbatch crystallization, hanging drop vapor diffusion method
-
recombinant enzyme in complex with N-acetylneuraminate and acetyl-D-mannosamine/pyruvate, soaking in the mother liquor containing 15% w/v PEG400, then 20% w/v PEG400, and subsequently for 5 min in 25% w/v PEG400 containing 75 mM Neu5Ac, X-ray diffraction structure determination and analysis
-
purified recombinant His-tagged wild-type enzyme, wild-type enzyme with Schiff base and in complex with pyruvate, mutant K164A enzyme, and mutant K164A in complex with N-acetylneuraminic acid and N-glycolylneuraminic acid, hanging drop vapour diffusion method, crystals of wild-type PmNAL from 21% PEG 1000, 150 mM NaCl, and 100 mM Na2HPO4/KH2PO4, pH 6.2. PmNAL K164A mutant in ligand-free from from 30% PEG 200, 100 mM NaCl, and acetate, pH 4.5. Crystals of the PmNAL K164A mutant bound to ligands are grown in 38% PEG 300, 0.01 M CaCl2, and 0.1 M sodium cacodylate, pH 6.5. The sialic acid concentration was 5 mM, X-ray diffraction structure determination and analysis at 1.75-2.10 A resolution, molecular replacement modeling
K0Y2E6
purified recombinant enzyme, hanging drop vapour diffusion method, 0.002-0.0025 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, is mixed with 0.0017-0.0022 ml of reservoir solution containing 25% w/v PEG 3350, 200 mM ammonium sulfate, 100 mM Bis-Tris pH 5.5, equilibration against 1 ml of reservoir solution, 8-20°C, method optimization, X-ray diffraction structure determination and analysis at 1.7 A resolution, molecular replacement
purified recombinant wild-type enzyme and mutants K165C variant and K165-gamma-thialysine, alone or in complex with pyruvate, hanging drop vapour diffusion method, mixing of 0.002 ml of protein solution containing 8 mg/ml protein in 50 mM, pH 7.4, with 0.002 ml of reservoir solution containing 100 mM Tris-HCl, pH 7.0-8.5, 200 mM NaCl, and 18-28% w/v PEG 3350, pyruvate complexes of the wild-type and K165-gamma-thialysine mutant enzymes crystals are soaked in the mother liquor containing 100 mM sodium pyruvate and 15% v/v PEG 400 for 1 min before being sequentially transferred to mother liquor with 5% increments in PEG 400 concentration. The final soak contains the mother liquor containing 100 mM sodium pyruvate and 25% v/v PEG 400, 18°C, X-ray diffraction structure determination and analysis at about 2.0 A resolution, molecular replacement
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
purified recombinant enzyme, 24 h, 4°C, different buffers, over 70% activity remains
727332
6.5 - 11
-
about 80% activity (synthesis of N-acetylneuraminic acid) after 15 days at pH 8.0-10.0 and 37°C, 60% activity (synthesis of N-acetylneuraminic acid) after 15 days at pH 11.0 and 37°C
713843
7 - 10.5
-
spore-displayed N-acetyl-D-neuraminic acid aldolase is stable for 24 hours at 50°C
713852
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
purified recombinant His-tagged enzyme, pH 7.0, completely stable over 140-160 min
37
50
60
70
80
additional information
37
-
in 50 mM Tris/HCl, pH 8, 25 mM MgCl2, 1 mM PMSF stable for at least 24 h
50
-
cross-linked enzyme aggregates, stable at pH 9.0 for 6 hours as the soluble enzyme
60
purified recombinant His-tagged enzyme, pH 7.0, 120 min, 60% activity remaining
70
-
50% loss of activity after 10 min, in presence of 80 mM pyruvate full activity retained after 1 h
70
purified recombinant His-tagged enzyme, pH 7.0, inactivation within 60 min
80
-
77% loss of activity after 10 min, in presence of 5 mM pyruvate 8% loss of activity after 10 min
80
purified recombinant His-tagged enzyme, pH 7.0, inactivation within 10 min
additional information
-
thermostability of enzyme produced by recombinant Serratia liquefaciens is higher by about 10°C than thermostability of enzyme produced by recombinant E. coli
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Amberzyme oxirane resin-immobilized NAL can be used up to five reaction cycles without loss of activity or significant decrease of the conversion rate, the activity yield of immobilized NAL is approximately 10% of the free enzyme
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to illumination in presence of Rose Bengal
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM Tris/HCl, pH 8, 25 mM MgCl2, 1 mM PMSF, 20% v/v glycerol, stable under prolonged storage
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
100-kDa ultrafiltration step, 65°C heat shock step and Ni2+ chelating affinity chromatography
-
recombinant enzyme from Escherichia coli strain BL21(DE3) by anion exchange and hydrophobic interaction chromatography, and gel filtration to over 95% purity
recombinant His-tagged enzyme 7.5fold from Escherichia coli strain Rosetta (DE3) pLys by ultrafiltration, nickel affinity chromatography, and gel filtration, to homogeneity
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
K0Y2E6
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 recombinant Escherichia coli strains capable of expressing N-acetyl-D-glucosamine 2-epimerase and N-acetyl-D-neuraminic acid aldolase are constructed based on a highly efficient temperature-responsive expression system which is safe compared to chemical-induced systems and coupled in N-acetyl-D-neuraminic acid production
-
a Bacillus subtilis outer spore coat protein fusion expressed in Bacillus subtilis WB600 results in a spore-displayed N-acetyl-D-neuraminic acid aldolase
-
cloning and recombinant expression in Escherichia coli strain BL21(DE3)
-
expressed in Bright Yellow 2 (BY2) tobacco cells and Medicago sativa cytosol
-
expression in Escherichia coli
gene nal, co-expression in Escherichia coli strain Rosetta (DE3) pLysS with N-acetylglucosamine 2-epimerase from Synechocystis sp. PCC 6803 (snAGE) or Anabaena sp. CH1 (anAGE)
-
gene nanA, DNA and amino acid sequence determination and analysis, sequence comparison, expression in Escherichia coli strain BL21(DE3)
gene nanA, recombinant expression of His6-tagged wild-type and mutant enzymes from plasmid pKK223-3 in Escherichia coli strain BL21(DE3)
gene ScNAL, sequence comparison, expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3) pLys
His-tagged version expressed in Escherichia coli BL21(DE3)pLys
-
recombinant His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
K0Y2E6
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene npl is downregulated by 17beta-estradiol
gene npl is significantly upregulated by progesterone. Progesterone receptor antagonist RU486 blocks the upregulation of Npl in both preimplantation uterus and progesterone-treated ovariectomized uterus
gene npl is downregulated by 17beta-estradiol
-
-
gene npl is significantly upregulated by progesterone. Progesterone receptor antagonist RU486 blocks the upregulation of Npl in both preimplantation uterus and progesterone-treated ovariectomized uterus
-
gene npl is significantly upregulated by progesterone. Progesterone receptor antagonist RU486 blocks the upregulation of Npl in both preimplantation uterus and progesterone-treated ovariectomized uterus
-
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E188D
-
cleaves 5-N-acetyl-9-O-acetylneuraminic acid as good as N-acetylneuraminic acid
E188Q
-
cleaves 5-N-acetyl-9-O-acetylneuraminic acid as good as N-acetylneuraminic acid
D191P
-
ratio of turnover-number to KM-value for (2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid is 1.4fold higher than the wild-type ratio
E192A
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E192C
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E192D
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E192F
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E192G
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E192H
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E192I
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E192K
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E192L
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E192M
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E192N
E192P
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E192Q
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E192R
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E192S
E192T
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E192V
E192W
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E192Y
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E60A/Y98H/F115L/N153Y/D150G/V251I/V265I/Y281C/N153Y
-
KM-value for N-acetyl-D-neuraminic acid is 5.9fold higher than the wild-type value, turnover-number for N-acetyl-D-neuraminic acid is 14% of the wild-type value, KM-value for N-acetyl-L-neuraminic acid is 7.6fold higher than the wild-type value, turnover-number for N-acetyl-L-neuraminic acid is 100fold higher than the wild-type value, KM-value for D-3-deoxy-manno-2-octulosonic acid is 83% of the wild-type value, turnover-number for D-3-deoxy-manno-2-octulosonic acid is 7.4fold higher than wild-type value, KM-value for L-3-deoxy-manno-2-octulosonic acid is 37% of the wild-type value, turnover-number for L-3-deoxy-manno-2-octulosonic acid is 9.5fold higher than wild-type value. kcat/KM for N-acetyl-D-neuraminic acid is 40.4fold lower than the wild-type value, kcat/KM for N-acetyl-D-neuraminic acid is 20fold higher than the wild-type value, kcat/KM for L-3-deoxy-manno-2-octulosonic acid is 24.7fold higher than the wild-type value
L171N/I229N
-
the mutant shows decreased kcat compared to the wild type enzyme
L199N/I229D
-
the mutant shows decreased kcat compared to the wild type enzyme
L199N/I229N
-
the mutant shows decreased kcat compared to the wild type enzyme
L199N/I229R
-
the mutant shows increased kcat compared to the wild type enzyme
L199R/I229N
-
the mutant shows increased kcat compared to the wild type enzyme
S208G
-
ratio of turnover-number to KM-value for N-acetyl-D-neuraminic acid is 2.5fold lower than the wild-type ratio, ratio of turnover-number to KM-value for (2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid is 1.5fold higher than the wild-type ratio
Y98H/F115L
-
KM-value for N-acetyl-D-neuraminic acid is 81% of the wild-type value, turnover-number for N-acetyl-D-neuraminic acid isnearly identical to wild-type value, KM-value for D-3-deoxy-manno-2-octulosonic acid is 89% of the wild-type value, turnover-number for D-3-deoxy-manno-2-octulosonic acid is 1.25fold higher than wild-type value, KM-value for L-3-deoxy-manno-2-octulosonic acid is 1.9fold higher than the wild-type value, turnover-number for L-3-deoxy-manno-2-octulosonic acid is identical to wild-type value. kcat/KM for N-acetyl-D-neuraminic acid is 1.1fold higher than the wild-type ratio, kcat/Km for D-3-deoxy-manno-2-octulosonic acid is 1.4fold higher than the wild-type ratio, kcat/KM for L-3-deoxy-manno-2-octulosonic acid is 1.8fold lower than the wild-type ratio
Y98H/F115L/N153Y/V251I/V265I/Y281C
-
KM-value for N-acetyl-D-neuraminic acid is 3.9fold higher than the wild-type value, turnover-number for N-acetyl-D-neuraminic acid is 16% of the wild-type value, KM-value for N-acetyl-L-neuraminic acid is 2.6fold higher than the wild-type value, turnover-number for N-acetyl-L-neuraminic acid is 100fold higher than the wild-type value, KM-value for D-3-deoxy-manno-2-octulosonic acid is 46% of the wild-type value, turnover-number for D-3-deoxy-manno-2-octulosonic acid is 4.36fold higher than wild-type value, KM-value for L-3-deoxy-manno-2-octulosonic acid is 32% of the wild-type value, turnover-number for L-3-deoxy-manno-2-octulosonic acid is 3.8fold higher than wild-type value. kcat/Km for N-acetyl-D-neuraminic acid is 23.8fold lower than the wild-type value, kcat/Km for N-acetyl-D-neuraminic acid is 20fold higher than the wild-type value, kcat/Km for D-3-deoxy-manno-2-octulosonic acid is 9.3fold higher than the wild-type value
Y98H/F115L/V251I
-
KM-value for N-acetyl-D-neuraminic acid is 1.5fold higher than the wild-type value, turnover-number for N-acetyl-D-neuraminic acid is 92% of the wild-type value, KM-value for N-acetyl-L-neuraminic acid is 84fold higher than the wild-type value, turnover-number for N-acetyl-L-neuraminic acid is 22.5fold higher than the wild-type value, KM-value for D-3-deoxy-manno-2-octulosonic acid is nearly identical to the wild-type value, turnover-number for D-3-deoxy-manno-2-octulosonic acid is 2.3fold higher than wild-type value, KM-value for L-3-deoxy-manno-2-octulosonic acid is 1.2fold higher than the wild-type value, turnover-number for L-3-deoxy-manno-2-octulosonic acid is 1.7fold higher than wild-type value. kcat/KM for N-acetyl-D-neuraminic acid is 1.6fold lower than the wild-type value, kcat/KM for N-acetyl-D-neuraminic acid is 5fold lower than the wild-type value, kcat/KM for D-3-deoxy-manno-2-octulosonic acid is 2.2fold higher than the wild-type value, kcat/KM for L-3-deoxy-manno-2-octulosonic acid is 1.4fold higher than the wild-type value
Y98H/F115L/V251I/V265I
-
KM-value for N-acetyl-D-neuraminic acid is 4.5fold higher than the wild-type value, turnover-number for N-acetyl-D-neuraminic acid is 45% of the wild-type value, KM-value for N-acetyl-L-neuraminic acid is 28.9fold higher than the wild-type value, turnover-number for N-acetyl-L-neuraminic acid is 34fold higher than the wild-type value, KM-value for D-3-deoxy-manno-2-octulosonic acid is 25% of the wild-type value, turnover-number for D-3-deoxy-manno-2-octulosonic acid is 2.6fold higher than wild-type value, KM-value for L-3-deoxy-manno-2-octulosonic acid is 36% of the wild-type value, turnover-number for L-3-deoxy-manno-2-octulosonic acid is 2.3fold higher than wild-type value. kcat/Km for N-acetyl-D-neuraminic acid is 22.4fold lower than the wild-type value, kcat/Km for N-acetyl-D-neuraminic acid is 2fold higher than the wild-type value
L171N/I229N
Escherichia coli W3110 / ATCC 27325
-
the mutant shows decreased kcat compared to the wild type enzyme
-
L199N/I229D
Escherichia coli W3110 / ATCC 27325
-
the mutant shows decreased kcat compared to the wild type enzyme
-
L199N/I229N
Escherichia coli W3110 / ATCC 27325
-
the mutant shows decreased kcat compared to the wild type enzyme
-
L199N/I229R
Escherichia coli W3110 / ATCC 27325
-
the mutant shows increased kcat compared to the wild type enzyme
-
L199R/I229N
Escherichia coli W3110 / ATCC 27325
-
the mutant shows increased kcat compared to the wild type enzyme
-
E192N
-
the turnover-number for sialic acid is 65% of the wild-type value, the Km-value for sialic acid is 8.6fold higher than the wild-type value, the turnover-number for (2R,3R,4R)-6-[(aminooxy)carbonyl]-3,4,6-trihydroxy-N-propyltetrahydro-2H-pyran-2-carboxamide is 57% of the wild-type value, the KM-value for (2R,3R,4R)-6-[(aminooxy)carbonyl]-3,4,6-trihydroxy-N-propyltetrahydro-2H-pyran-2-carboxamide is 28.2fold lower than the wild-type value. The mutant enzyme is most efficient in catalysis of the synthesis of the tertiary amides (4S,5R,6R)-6-[(diethylamino)carbonyl]-2,4,5-trihydroxytetrahydro-2H-pyran-2-carboxylic acid, (4R,5R,6R)-6-[(diethylamino)carbonyl]-2,4,5-trihydroxytetrahydro-2H-pyran-2-carboxylic acid, (4S,5R,6R)-2,4,5-trihydroxy-6-{[methyl(propyl)amino]carbonyl}tetrahydro-2H-pyran-2-carboxylic acid, (4R,5R,6R)-2,4,5-trihydroxy-6-{[methyl(propyl)amino]carbonyl}tetrahydro-2H-pyran-2-carboxylic acid, (4S,5R,6R)-6-[(dipropylamino)carbonyl]-2,4,5-trihydroxytetrahydro-2H-pyran-2-carboxylic acid, (4R,5R,6R)-6-[(dipropylamino)carbonyl]-2,4,5-trihydroxytetrahydro-2H-pyran-2-carboxylic acid, (4S,5R,6R)-6-[(dibutylamino)carbonyl]-2,4,5-trihydroxytetrahydro-2H-pyran-2-carboxylic acid, (4R,5R,6R)-6-[(dibutylamino)carbonyl]-2,4,5-trihydroxytetrahydro-2H-pyran-2-carboxylic acid, (4S,5R,6R)-2,4,5-trihydroxy-6-(pyrrolidin-1-ylcarbonyl)tetrahydro-2H-pyran-2-carboxylic acid, (4R,5R,6R)-2,4,5-trihydroxy-6-(pyrrolidin-1-ylcarbonyl)tetrahydro-2H-pyran-2-carboxylic acid, (4S,5R,6R)-2,4,5-trihydroxy-6-(piperidin-1-ylcarbonyl)tetrahydro-2H-pyran-2-carboxylic acid, (4R,5R,6R)-2,4,5-trihydroxy-6-(piperidin-1-ylcarbonyl)tetrahydro-2H-pyran-2-carboxylic acid, (4S,5R,6R)-2,4,5-trihydroxy-6-(morpholin-4-ylcarbonyl)tetrahydro-2H-pyran-2-carboxylic acid, (4R,5R,6R)-2,4,5-trihydroxy-6-(morpholin-4-ylcarbonyl)tetrahydro-2H-pyran-2-carboxylic acid
F252A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F252Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S47A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S47C
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S47T
-
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
T167A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T167S
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
T48A
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T48S
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y110A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y110F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y137F
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K164A
K0Y2E6
site-directed mutagenesis, determiniation of three structures of the K164A variant: one in the absence of substrates and two binary complexes with N-acetylneuraminic acid and N-glycolylneuraminic acid. Both sialic acids bind to the active site in the open-chain ketone form of the monosaccharide, every hydroxyl group of the linear sugars makes hydrogen bond interactions with the enzyme
C118A
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
C118S
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
C238A
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
C238S
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
C270A
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
C270S
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
C82A
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
C82S
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
K165C
site-directed mutagenesis to introduce a cysteine in place of Lys165 in the enzyme active site and complete conversion of the cysteine into gamma-thialysine through dehydroalanine as by chemical mutagenesis, ESI-mass spectrometry and kinetic characterisation, the K165C variant is severely impaired in catalysis, kcat/Km is reduced 720fold compared with wild-type
K165Dha
site-directed mutagenesis to introduce a cysteine in place of Lys165 in the enzyme active site and complete conversion of the cysteine into gamma-thialysine, Dha, through dehydroalanine as by chemical mutagenesis, ESI-mass spectrometry and kinetic characterisation, the enzyme containing gamma-thialysine regains 17-30% of the wild-type activity
C238S
-
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
-
C270S
-
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
-
C82A
-
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
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C82S
-
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
-
K165C
-
site-directed mutagenesis to introduce a cysteine in place of Lys165 in the enzyme active site and complete conversion of the cysteine into gamma-thialysine through dehydroalanine as by chemical mutagenesis, ESI-mass spectrometry and kinetic characterisation, the K165C variant is severely impaired in catalysis, kcat/Km is reduced 720fold compared with wild-type
-
additional information
E192N
-
ratio of turnover-number to KM-value for N-acetyl-D-neuraminic acid is 13.4fold lower than the wild-type ratio, ratio of turnover-number to KM-value for (2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid is 48.7fold higher than the wild-type ratio
E192N
-
the mutant has a 6fold higher specificity (kcat/Km) for dipropylaminocarbonyl-substituted derivatives than wild type enzyme
E192N
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strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E192S
-
ratio of turnover-number to KM-value for N-acetyl-D-neuraminic acid is 3.9fold lower than the wild-type ratio, ratio of turnover-number to KM-value for (2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid is 32.2fold higher than the wild-type ratio
E192S
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
E192V
-
ratio of turnover-number to KM-value for N-acetyl-D-neuraminic acid is 17.9fold lower than the wild-type ratio, ratio of turnover-number to KM-value for (2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid is 39.3fold higher than the wild-type ratio
E192V
-
strong interaction of Glu192 (wild type) with hydroxyl groups at C8 and C9 of N-acetylneuraminic acid
additional information
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directed evolution of D-sialic acid aldolase to L-3-deoxy-manno-2-octulosonic acid (L-KDO) aldolase
additional information
-
synthesis of N-acetylneuraminic acid from N-acetylglucosamine and pyruvate by constructing and co-expressing a polycistronic plasmid encoding an N-acetylglucosamine 2-epimerase gene from Synechocystis sp. PCC 6803 (snAGE) or Anabaena sp. CH1 (anAGE) and the Escherichia coli N-acetylneuraminic acid lyase gene. Construction of four polycistronic plasmids in which the positions of AGE gene differ with respect to Nal gene, plasmid pET-28a-Nal-anAGE with anAGE gene located next to Nal gene produces the highest amount of N-acetylneuraminic acid, overview. anAGE from Anabaena sp. CH1 shows much higher activity and productivity than snAGE from Synechocystis sp. PCC 6803
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type enzyme with various concentrations of urea in Tris·HCl buffer, 50 mM, pH 7.4, the refolded enzyme shows higher activity than the native wild-type enzyme
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
synthesis
analysis
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generation of a dynamic combinatorial library of sialic acid analogues using sialic acid aldolase
biotechnology
coupled bioconversion for preparation of N-acetyl-D-neuraminic acid using immobilized N-acetyl-D-glucosamine-2-epimerase and N-acetyl-D-neuraminic acid lyase, a two-step enzymatic system involving immobilized both enzymes is used for the conversion of GlcNAc to NeuAc in a single reactor, optimum ratio is 3-6.25 U/ml of N-acetyl-D-glucosamine-2-epimerase and 12.5-25 U/ml of N-acetyl-D-neuraminic acid lyase
biotechnology
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efficient method for N-acetyl-D-neuraminic acid production using coupled bacterial cells with a safe temperature-induced system, a precursor for producing many pharmaceutical drugs such as zanamivir which have been used in clinical trials to treat and prevent the infection with influenza virus, such as the avian influenza virus H5N1 and the current 2009 H1N1
biotechnology
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chemoenzymatic synthesis of N-acetyl-D-neuraminic acid from N-acetyl-D-glucosamine and pyruvate
synthesis
-
enzymatic synthesis of N-acetylneuraminic acid, large scale production using N-acetylneuraminate lyase and N-acetyl-D-glucosamine-2-epimerase
synthesis
-
enzymatic synthesis of N-acetylneuraminic acid with immobilized enzyme
synthesis
-
production of N-acetyl-D-neuraminic acid, which is the major representative of amino sugars. The synthesis of N-acetyl-D-neuraminic acid is of interest in studies towards inhibitors of neuraminidase, hemagglutinin and selectin-mediated leucocyte adhesion