2.5.1.56: N-acetylneuraminate synthase
This is an abbreviated version!
For detailed information about N-acetylneuraminate synthase, go to the full flat file.
Word Map on EC 2.5.1.56
-
2.5.1.56
-
n-acetylmannosamine
-
antifreeze
-
mannac
-
meningitidis
-
polysialic
-
neunacs
-
neuroinvasive
-
synthesis
-
cmp-sialic
-
2-epimerase
-
ice-binding
- 2.5.1.56
- n-acetylmannosamine
-
antifreeze
- mannac
- meningitidis
-
polysialic
-
neunacs
-
neuroinvasive
- synthesis
-
cmp-sialic
-
2-epimerase
-
ice-binding
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
Advanced search results
Subunits
Subunits on EC 2.5.1.56 - N-acetylneuraminate synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
dimer
homodimer
monomer
tetramer
additional information
2 * 45000, about, recombinant enzyme, SDS-PAGE, 2 * 41000, about, recombinant enzyme, HPLC/MS/ESI
homodimer
-
2 * 45000, about, recombinant enzyme, SDS-PAGE, 2 * 41000, about, recombinant enzyme, HPLC/MS/ESI
-
homodimer
2 * 38935, sequence calculation, 2 * 38000, about, recombinant enzyme, SDS-PAGE
homodimer
the enzyme comprises two distinct domains, an N-terminal catalytic (beta/alpha)8 barrel linked to a C-terminal antifreeze protein-like (AFPL) domain. Loss of the AFPL domain destabilizes the dimeric form of the enzyme nd renders it inactive. The AFPL domain plays a critical role for both the catalytic function and quaternary structure stability of N-acetylneuraminic acid synthase. The enzyme mutant G272Term lacking the AFPL domain is partly monomeric
homodimer
-
the enzyme comprises two distinct domains, an N-terminal catalytic (beta/alpha)8 barrel linked to a C-terminal antifreeze protein-like (AFPL) domain. Loss of the AFPL domain destabilizes the dimeric form of the enzyme nd renders it inactive. The AFPL domain plays a critical role for both the catalytic function and quaternary structure stability of N-acetylneuraminic acid synthase. The enzyme mutant G272Term lacking the AFPL domain is partly monomeric
-
the enzyme structure has a distinct domain architecture 4 without a cystathionine-beta-synthase domain (cystathionine-beta-synthetase domain), unlike domain architecture 3. The arginine essential for catalysis, that is present in antifreeze-like domain (block X), is not fully conserved in NeuB, but is replaced by a serine in domain architectures 3 and 4, three-dimensional structure comparison, and secondary structure element comparisons, detailed overview
additional information
-
the enzyme structure has a distinct domain architecture 4 without a cystathionine-beta-synthase domain (cystathionine-beta-synthetase domain), unlike domain architecture 3. The arginine essential for catalysis, that is present in antifreeze-like domain (block X), is not fully conserved in NeuB, but is replaced by a serine in domain architectures 3 and 4, three-dimensional structure comparison, and secondary structure element comparisons, detailed overview
additional information
-
the enzyme structure has a distinct domain architecture 4 without a cystathionine-beta-synthase domain (cystathionine-beta-synthetase domain), unlike domain architecture 3. The arginine essential for catalysis, that is present in antifreeze-like domain (block X), is not fully conserved in NeuB, but is replaced by a serine in domain architectures 3 and 4, three-dimensional structure comparison, and secondary structure element comparisons, detailed overview
-
additional information
the enzyme contains an antifreeze protein like (AFPL) domain, which extends from the C-terminal of the (beta/alpha)8 barrel containing the active site and contributes a highly conserved arginine, Arg314, into the active site of the opposing monomer chain
additional information
-
the enzyme contains an antifreeze protein like (AFPL) domain, which extends from the C-terminal of the (beta/alpha)8 barrel containing the active site and contributes a highly conserved arginine, Arg314, into the active site of the opposing monomer chain
additional information
-
the enzyme contains an antifreeze protein like (AFPL) domain, which extends from the C-terminal of the (beta/alpha)8 barrel containing the active site and contributes a highly conserved arginine, Arg314, into the active site of the opposing monomer chain
-