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Literature summary extracted from

  • Sulzenbacher, G.; Liu, Q.; Bennett, E.; Levery, S.; Bourne, Y.; Ponchel, G.; Clausen, H.; Henrissat, B.
    A novel alpha-N-acetylgalactosaminidase family with an NAD+-dependent catalytic mechanism suitable for enzymatic removal of blood group A antigens (2010), Biocatal. Biotransform., 28, 22-32.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.49 expression in Escherichia coli Elizabethkingia meningoseptica

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.49 native enzyme and in complex with alpha-N-acetylgalactosamine, to 2.3 and 2.4 A resolution, respectively. Each monomer of NagA consists of two closely associated domains, forming a narrow tunnel in which the NAD+ molecule is anchored. The NAD+ is embedded within a narrow tunnel, almost exclusively shielded from solvent. It is bound with its diphosphate group oriented towards the N-terminus of the first alpha-helix of the N-terminal dinucleotide-binding domain and has both the adenine ring and the nicotinamide ring in the anti conformation. No major structural changes are observed in NagA upon product binding Elizabethkingia meningoseptica

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.49 48500
-
 2 * 48500, SDS-PAGE Elizabethkingia meningoseptica
3.2.1.49 48500
-
 1 * 48500, SDS-PAGE Elizabethkingia meningoseptica
3.2.1.49 83000
-
 gel filtration Elizabethkingia meningoseptica

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.49 Elizabethkingia meningoseptica A4Q8F7 member of glycosyl hydrolase family 109
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.49
-
 Elizabethkingia meningoseptica

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.49 alpha-D-GalNAc-(1->3)-beta-D-GalNAc-(1->3)-alpha-D-Gal-(1->4)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-ceramide + H2O = D-GalNAc + beta-D-GalNAc-(1->3)-alpha-D-Gal-(1->4)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-ceramide a hydride at C3, activated by the interaction of the OH-3 hydroxyl with the conserved His228, is abstracted by NAD+ with oxidation of the OH-3 hydroxyl to a ketone. This activates H2 for proton abstraction by Tyr179, accompanied by elimination of the aglycone, thereby generating a 1,2-unsaturated intermediate. Water is then added to the anomeric center, followed by the reduction of the C3 ketone by the on-board NADH, completing the catalytic sequence and restoring NADH to NAD+ and the enzyme to its starting state to bind another substrate Elizabethkingia meningoseptica
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.49 2-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
-
 Elizabethkingia meningoseptica 2-nitrophenol + alpha-N-acetylgalactosamine
-
 ?
3.2.1.49 additional information enzyme efficiently cleaves blood group A antigen. Unusual catalytic mechanism involving NAD+. NagA might adopt a mechanism similar to that of glycosyl hydrolase family 4 enzymes utilizing an oxidation-elimination-addition-reduction sequence Elizabethkingia meningoseptica ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.49 dimer 2 * 48500, SDS-PAGE Elizabethkingia meningoseptica
3.2.1.49 monomer 1 * 48500, SDS-PAGE Elizabethkingia meningoseptica
3.2.1.49 More enzyme may exist both in the monomeric and dimeric form, depending on the salt concentration of the buffer solution Elizabethkingia meningoseptica

Synonyms

EC Number Synonyms Comment Organism
3.2.1.49 NagA
-
 Elizabethkingia meningoseptica

Cofactor

EC Number Cofactor Comment Organism Structure
3.2.1.49 NAD+ binds 1 NAD+ per subunit. The NAD+ cannot dissociate Elizabethkingia meningoseptica