2.5.1.56: N-acetylneuraminate synthase

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For detailed information about N-acetylneuraminate synthase, go to the full flat file.

Reaction

Synonyms

(NANA) condensing enzyme, EC 4.1.3.19, N-acetylneuraminate lyase synthase, N-acetylneuraminate pyruvate-lyase (pyruvate-phosphorylating), N-acetylneuraminic acid condensing enzyme, N-acetylneuraminic acid synthase, NANA condensing enzyme, NANA synthase, NANAS, NANS, NeuAc synthase, NeuB, NeuB1, NeuNAc synthase, NmeNANAS, sialic acid synthase, synthase, N-acetylneuraminate

ECTree

     2 Transferases

         2.5 Transferring alkyl or aryl groups, other than methyl groups

             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)

                2.5.1.56 N-acetylneuraminate synthase

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Results	in table
1	Activating Compound
1671	AA Sequence
6	Application
1	CAS Registry Number
8	Cloned(Commentary)
3	Crystallization (Commentary)
10	Disease/ Diagnostics
14	General Information
3	General Stability
27	Inhibitors
1	Ki Value [mM]
18	KM Value [mM]
2	Localization
23	Metals/Ions
20	Molecular Weight [Da]
15	Natural Substrates/ Products (Substrates)
52	Organism
6	Pathway
7	PDB ID
7	pH Optimum
4	pH Range
9	pH Stability
29	Protein Variants
8	Purification (Commentary)
2	Reaction
3	Reaction Type
35	Reference
4	Source Tissue
12	Specific Activity [micromol/min/mg]
1	Storage Stability
47	Substrates and Products (Substrate)
20	Subunits
39	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
3	Temperature Range [°C]
9	Temperature Stability [°C]
8	Turnover Number [1/s]

General Stability

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General Stability on EC 2.5.1.56 - N-acetylneuraminate synthase

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

a specific cleavage by endogenous proteases at Lys280 of the 40000 Da enzyme. Cleavage results in the formation of two inactive fragments of 33000 Da and 7000 Da. The fragmentation is associated with a significant change of the enzyme from a tetrameric to trimeric form, and alterations in both secondary and native quarternary structures

Escherichia coli

-

637323

expression of the native neuB gene product enzyme in E. coli results in a product that is prone to proteolysis during purification so the protein is tagged with a hexa-histidine tag at its N-terminus and rapidly purified

Streptococcus agalactiae

-

637325

phosphoenolpyruvate has a major effect on the thermal stability of the wild-type enzyme requiring the C-terminal AFPL domain

Neisseria meningitidis

H2VFG5

739614