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Information on EC 4.1.3.3 - N-acetylneuraminate lyase
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4.1.3.3 N-acetylneuraminate lyaseIUBMB Comments
This enzyme is involved in the degradation of N-acetylneuraminate. It is specific for the open form of the sugar. It also acts on N-glycoloylneuraminate and on O-acetylated sialic acids, other than 4-O-acetylated derivatives.
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Word Map
- 4.1.3.3
- mannac
-
2-epimerase
- n-acetylmannosamine
- aldolases
- dihydrodipicolinate
-
n-glycolylneuraminic
-
cmp-sialic
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3.2.1.18
- neu5gc
- dhdps
- synthesis
- biotechnology
- n-acylneuraminate
- analysis
- industry
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
Acetylneuraminate pyruvate-lyase, class I NAL, EcNanA, Lyase, acetylneuraminate, N-acetyl-d-neuraminic acid aldolase, N-acetyl-D-neuraminic acid lyase, N-Acetylneuraminate aldolase, N-Acetylneuraminate lyase, N-acetylneuraminate pyruvate lyase, N-Acetylneuraminate pyruvate-lyase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Acetylneuraminate pyruvate-lyase
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class I NAL
Lyase, acetylneuraminate
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N-acetyl-d-neuraminic acid aldolase
N-acetyl-D-neuraminic acid lyase
N-Acetylneuraminate aldolase
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N-Acetylneuraminate lyase
N-acetylneuraminate pyruvate lyase
N-Acetylneuraminate pyruvate-lyase
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N-Acetylneuraminic acid aldolase
N-Acetylneuraminic acid lyase
N-Acetylneuraminic aldolase
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N-Acetylneuraminic lyase
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NAL
NALase
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NanA
NANA lyase
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Neu5Ac aldolase
Neu5Ac lyase
NeuAc aldolase
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Neuraminate aldolase
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Neuraminic acid aldolase
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Neuraminic aldolase
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NPL
Sialate lyase
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Sialic acid aldolase
Sialic aldolase
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N-Acetylneuraminate lyase
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N-acetylneuraminate pyruvate lyase
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N-Acetylneuraminic acid aldolase
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N-Acetylneuraminic acid lyase
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NPL
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Sialic acid aldolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
aceneuramate = N-acetyl-D-mannosamine + pyruvate
mechanism
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aceneuramate = 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
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aceneuramate = N-acetyl-D-mannosamine + pyruvate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aldol addition
C-C-bond cleavage
condensation
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elimination
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of an oxo-acid, C-C bond cleavage
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
aceneuramate pyruvate-lyase (N-acetyl-D-mannosamine-forming)
This enzyme is involved in the degradation of N-acetylneuraminate. It is specific for the open form of the sugar. It 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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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
(2R,3R,4R)-6-[(aminooxy)carbonyl]-3,4,6-trihydroxy-N-propyltetrahydro-2H-pyran-2-carboxamide
?
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?
(2S,4S,5R,6R)-5-(acetylamino)-6-[(dipropylamino)carbonyl]-2,4-dihydroxytetrahydro-pyran-2-carboxylic acid
?
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?
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
pyruvate + (2R,3S)-2,3-dihydroxy-4-oxo-N,N-dipropylbutanamide
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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
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36% yield
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?
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
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34% yield
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?
3-bromo-3-deoxy-D-mannose + pyruvate
?
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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
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?
4-O-alpha-D-galactopyranosyl-D-mannopyranose + pyruvate
3-deoxy-7-O-alpha-D-galactopyranosyl-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
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5% yield
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?
4-O-beta-D-galactopyranosyl-D-mannopyranose + pyruvate
3-deoxy-7-O-beta-D-galactopyranosyl-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
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38% yield
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?
4-O-beta-D-glucopyranosyl-D-mannopyranose + pyruvate
3-deoxy-7-O-beta-D-glucopyranosyl-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
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35% yield
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?
5-N-acetyl-4-O-acetylneuraminic acid
?
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22% the activity with N-acetylneuraminic acid
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?
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
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62% yield
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?
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
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85% yield
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?
5-O-methyl-N-acetyl-D-mannosamine + pyruvate
8-O-methyl-N-acetylneuraminate
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?
6-O-alpha-D-galactopyranosyl-D-mannopyranose + pyruvate
3-deoxy-9-O-alpha-D-galactopyranosyl-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
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81% yield
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?
6-O-alpha-D-glucopyranosyl-D-mannopyranose + pyruvate
3-deoxy-9-O-alpha-D-glucopyranosyl-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
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65% yield
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?
6-O-alpha-D-mannopyranosyl-D-mannopyranose + pyruvate
3-deoxy-9-O-alpha-D-mannopyranosyl-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
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78% yield
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?
6-O-beta-D-glucopyranosyl-D-mannopyranose + pyruvate
3-deoxy-9-O-beta-D-glucopyranosyl-D-glycero-beta-D-galacto-non-2-ulopyranosonic acid
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83% yield
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?
D-arabinose + pyruvate
D-3-deoxy-manno-2-octulosonic acid
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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
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r
D-glucose + pyruvate
?
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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
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?
D-gulose + pyruvate
?
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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
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?
D-mannosamine + pyruvate
?
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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
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?
D-mannose + pyruvic acid
2-keto-3-deoxy-D-glycero-D-galacto-nonopyranulosonic acid
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?
D-talose + pyruvate
?
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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
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?
L-arabinose + pyruvate
L-3-deoxy-manno-2-octulosonic acid
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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
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r
L-mannose + pyruvate
?
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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
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?
N-acetyl-D-mannosamine + pyruvate
N-acetyl-D-neuraminic acid
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r
N-acetyl-L-mannosamine + pyruvate
N-acetyl-L-neuraminic acid
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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
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r
pyruvate + alpha-D-Galp-(1,6)-D-Manp
alpha-D-Galp-(1,9)-D-deoxyneuraminic acid
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?
2-deoxy-D-glucose + pyruvate
?
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33% activity compared to N-acetylneuraminate
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r
2-deoxy-D-glucose + pyruvate
?
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33% activity compared to N-acetylneuraminate
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r
2-deoxy-D-glucose + pyruvate
?
1.2% activity compared to N-acetylneuraminate
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r
2-deoxy-D-glucose + pyruvate
?
Limosilactobacillus antri DSMZ 16041
1.2% activity compared to N-acetylneuraminate
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r
5-N-acetyl-9-O-acetylneuraminic acid
?
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54% the activity with N-acetylneuraminic acid
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?
5-N-acetyl-9-O-acetylneuraminic acid
?
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32.45% the activity with N-acetylneuraminic acid
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?
5-N-acetyl-9-O-acetylneuraminic acid
?
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45% the activity with N-acetylneuraminic acid
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?
D-arabinose + pyruvate
3-deoxy-D-manno-2-octulosonic acid
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1.0% activity compared to N-acetylneuraminate
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r
D-arabinose + pyruvate
3-deoxy-D-manno-2-octulosonic acid
1.5% activity compared to N-acetylneuraminate
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r
D-mannose + pyruvate
?
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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
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?
D-mannose + pyruvate
?
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95% activity compared to N-acetylneuraminate
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r
D-mannose + pyruvate
?
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95% activity compared to N-acetylneuraminate
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r
D-mannose + pyruvate
?
10% activity compared to N-acetylneuraminate
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r
D-mannose + pyruvate
?
Limosilactobacillus antri DSMZ 16041
10% activity compared to N-acetylneuraminate
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r
D-xylose + pyruvate
?
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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
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?
D-xylose + pyruvate
?
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2.4% activity compared to N-acetylneuraminate
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r
D-xylose + pyruvate
?
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2.4% activity compared to N-acetylneuraminate
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r
D-xylose + pyruvate
?
0.6% activity compared to N-acetylneuraminate
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r
D-xylose + pyruvate
?
Limosilactobacillus antri DSMZ 16041
0.6% activity compared to N-acetylneuraminate
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r
L-gulose + pyruvate
?
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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
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?
L-gulose + pyruvate
?
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3.6% activity compared to N-acetylneuraminate
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r
L-gulose + pyruvate
?
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3.6% activity compared to N-acetylneuraminate
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r
L-gulose + pyruvate
?
0.7% activity compared to N-acetylneuraminate
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r
L-gulose + pyruvate
?
Limosilactobacillus antri DSMZ 16041
0.7% activity compared to N-acetylneuraminate
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r
N-acetyl-D-mannosamine + pyruvate
N-acetylneuraminate
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r
N-acetyl-D-mannosamine + pyruvate
N-acetylneuraminate
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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
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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
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r
N-acetyl-D-mannosamine + pyruvate
N-acetylneuraminate
reversible aldol condensation of pyruvate and N-acetyl-D-mannosamine
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r
N-acetyl-D-mannosamine + pyruvate
N-acetylneuraminate
reversible aldol condensation of pyruvate and N-acetyl-D-mannosamine
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r
N-Acetyl-D-mannosamine + pyruvate
N-Acetylneuraminic acid
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r
N-Acetyl-D-mannosamine + pyruvate
N-Acetylneuraminic acid
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r
N-acetyl-D-neuraminic acid
N-acetyl-D-mannosamine + pyruvate
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in presence of excess pyruvate the equilibrium may be driven in the direction of aldol product formation
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r
N-acetyl-D-neuraminic acid
N-acetyl-D-mannosamine + pyruvate
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-
-
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r
N-acetyl-D-neuraminic acid
pyruvate + N-acetyl-D-mannosamine
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-
-
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r
N-acetyl-D-neuraminic acid
pyruvate + N-acetyl-D-mannosamine
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-
-
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r
N-acetyl-neuraminic acid
N-acetyl-D-mannosamine + pyruvate
-
-
-
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r
N-Acetylmannosamine + pyruvate
?
-
N-acetylneuraminic acid is intermediate for colomic acid biosynthesis
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-
?
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
-
-
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r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
-
-
-
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r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
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-
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r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
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the enzyme catalyzes the reversible condensation of pyruvate with N-acetyl-D-mannosamine to yield the sialic acid N-acetylneuraminic acid
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r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
-
100% activity
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
-
100% activity
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
100% activity
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
Limosilactobacillus antri DSMZ 16041
100% activity
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
reversible aldol cleavage of N-acetylneuraminic acid
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-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
-
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
-
-
-
?
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
-
-
?
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-acetylneuraminic acid
pyruvate + N-acetyl-D-mannosamine
-
-
-
-
r
N-acetylneuraminic acid
pyruvate + N-acetyl-D-mannosamine
-
-
-
-
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
?
-
-
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 SUBSTRATE
NATURAL 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
N-Acetylneuraminic acid
N-Acetyl-D-mannosamine + pyruvate
-
regulation of sialic acid metabolism
-
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
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-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
-
-
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
-
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
-
100% activity
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
-
100% activity
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
100% activity
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
Limosilactobacillus antri DSMZ 16041
100% activity
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
-
-
-
?
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
-
-
?
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
Ba2+
about 170% activity at 5 mM and pH 7.5 for N-acetylneuraminate synthesis
Co2+
about 225% activity at 5 mM and pH 7.5 for N-acetylneuraminate synthesis
Fe3+
about 125% activity at 5 mM and pH 7.5 for N-acetylneuraminate synthesis
Mg2+
about 270% activity at 5 mM and pH 7.5 for N-acetylneuraminate synthesis
Ni2+
additional information
Ni2+
about 220% activity at 5 mM and pH 7.5 for N-acetylneuraminate synthesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CTAB
about 30% residual activity at 5 mM and pH 7.5 for N-acetylneuraminate synthesis and almost complete inhibition at 5 mM for N-acetylneuraminate cleavage
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
SDS
about 30% residual activity at 5 mM and pH 7.5 for N-acetylneuraminate synthesis and almost complete inhibition at 5 mM for N-acetylneuraminate cleavage
Zn2+
about 25% residual activity at 5 mM and pH 7.5 for N-acetylneuraminate synthesis and almost complete inhibition at 5 mM and pH 7.5 for N-acetylneuraminate cleavage
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Triton X-100
about 150% activity at 5 mM and pH 8.5 for N-acetylneuraminate synthesis and about 220% activity at 5 mM and pH 8.5 for N-acetylneuraminate cleavage
EDTA
about 120% activity at 5 mM and pH 7.5 for N-acetylneuraminate synthesis and about 150% activity at 5 mM and pH 8.5 for N-acetylneuraminate cleavage
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma, Hepatocellular
[On the activity of neuraminic acid aldolase and neuraminidase in the cells of ascite and solid forms of hepatoma 22 in mice]
Foot-and-Mouth Disease
Active protein aggregates induced by terminally attached self-assembling peptide ELK16 in Escherichia coli.
Influenza, Human
Synthesis of screening substrates for the directed evolution of sialic acid aldolase: towards tailored enzymes for the preparation of influenza A sialidase inhibitor analogues.
Sialic Acid Storage Disease
Sialic acid catabolism by N-acetylneuraminate pyruvate lyase is essential for muscle function.
Tuberculosis
Inhibiting dihydrodipicolinate synthase across species: towards specificity for pathogens?
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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
0.2
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
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
0.4
(5R,6R)-7-(dipropylamino)-4,5,6-trihydroxy-2,7-dioxoheptanoic acid
-
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
333
N-acetyl-D-mannosamine
wild type enzyme, at pH 7.0 and 37°C
915
N-acetyl-D-mannosamine
mutant enzyme P193Y, at pH 7.0 and 37°C
3200
N-acetyl-D-mannosamine
mutant enzyme G210S/Y213G, at pH 7.0 and 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
0.27
N-acetylneuraminate
mutant enzyme P193Y, at pH 7.0 and 37°C
1.1
N-acetylneuraminate
wild type enzyme, at pH 7.0 and 37°C
1.2
N-acetylneuraminate
mutant enzyme G211S, at pH 7.0 and 37°C
2
N-acetylneuraminate
recombinant His-taggged enzyme, pH 7.0, 37°C
2
N-acetylneuraminate
mutant enzyme G210S/Y213G, at pH 7.0 and 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
3.2
N-acetylneuraminate
at 30°C, pH not specified in the publication
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
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
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
2.4
N-acetyl-D-mannosamine
mutant enzyme P193Y, at pH 7.0 and 37°C
4.5
N-acetyl-D-mannosamine
recombinant His-taggged enzyme, pH 7.0, 37°C
5.4
N-acetyl-D-mannosamine
wild type enzyme, at pH 7.0 and 37°C
15.3
N-acetyl-D-mannosamine
mutant enzyme G210S/Y213G, at pH 7.0 and 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
0.02
N-acetyl-L-neuraminic acid
-
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
0.032
N-acetylneuraminate
mutant enzyme G211S, at pH 7.0 and 37°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
0.13
N-acetylneuraminate
mutant enzyme P193Y, at pH 7.0 and 37°C
0.29
N-acetylneuraminate
mutant enzyme L199N/I229D, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
0.47
N-acetylneuraminate
mutant enzyme G210S/Y213G, at pH 7.0 and 37°C
0.664
N-acetylneuraminate
mutant enzyme L199N/I229N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C
1.9
N-acetylneuraminate
wild type enzyme, at pH 7.0 and 37°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
22.1
N-acetylneuraminate
at 30°C, pH not specified in the publication
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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
0.002
N-acetyl-D-mannosamine
mutant enzyme P193Y, at pH 7.0 and 37°C
0.004
N-acetyl-D-mannosamine
mutant enzyme G210S/Y213G, at pH 7.0 and 37°C
0.0074
N-acetyl-D-mannosamine
-
cross-linked enzyme aggregates, pH 7.5, 37°C
0.016
N-acetyl-D-mannosamine
wild type enzyme, at pH 7.0 and 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
0.026
N-acetylneuraminate
mutant enzyme G211S, at pH 7.0 and 37°C
0.23
N-acetylneuraminate
mutant enzyme G210S/Y213G, at pH 7.0 and 37°C
0.48
N-acetylneuraminate
mutant enzyme P193Y, at pH 7.0 and 37°C
1.7
N-acetylneuraminate
wild type enzyme, at pH 7.0 and 37°C
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
0.08
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
0.71
pyruvate
mutant enzyme G210S/Y213G, at pH 7.0 and 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.39
(2R)-sialic acid alditol
at 30°C, pH not specified in the publication
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 - 7
6.5 - 7
7.2
7.4
7.5
7.5 - 8
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
40
45
50
60
70
75
40
for N-acetylneuraminate cleavage at pH 7.5 and N-acetylneuraminate synthesis at pH 8.5
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
subspecies aureus, methicillin-resistant, gene nanA
UniProt
brenda
-
-
-
brenda
the sequence of the cloned gene differs on six bases, T228C, T303C, C624T, G777A, C786T and C832T
UniProt
brenda
subspecies aureus, methicillin-resistant, gene nanA
UniProt
brenda
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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
brenda
-
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
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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
-
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
-
Show AA Sequence and Transmembrane Helices (2703 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM