KEGG   ENZYME: 3.2.1.97Help
Entry
EC 3.2.1.97                 Enzyme                                 

Name
endo-alpha-N-acetylgalactosaminidase;
endo-alpha-acetylgalactosaminidase;
endo-alpha-N-acetyl-D-galactosaminidase;
mucinaminylserine mucinaminidase;
D-galactosyl-3-(N-acetyl-alpha-D-galactosaminyl)-L-serine mucinaminohydrolase;
endo-alpha-GalNAc-ase;
glycopeptide alpha-N-acetylgalactosaminidase;
D-galactosyl-N-acetyl-alpha-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
BRITE hierarchy
Sysname
glycopeptide-D-galactosyl-N-acetyl-alpha-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase
Reaction(IUBMB)
beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-[glycoprotein]-L-serine/L-threonine + H2O = beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine + [glycoprotein]-L-serine/L-threonine [RN:R04527 R06140]
Reaction(KEGG)
Substrate
beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-[glycoprotein]-L-serine/L-threonine;
H2O [CPD:C00001]
Product
beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine [CPD:C07278];
[glycoprotein]-L-serine/L-threonine
Comment
The enzyme catalyses the liberation of Gal-(1->3)-beta-GalNAc alpha-linked to serine or threonine residues of mucin-type glycoproteins. EngBF from the bacterium Bifidobacterium longum specifically acts on core 1-type O-glycan to release the disaccharide Gal-(1->3)-beta-GalNAc. The enzymes from the bacteria Clostridium perfringens, Enterococcus faecalis, Propionibacterium acnes and Alcaligenes faecalis show broader specificity (e.g. they can also release the core 2 trisaccharide Gal-(1->3)-beta-(GlcNAc-(1->6)-beta)-GalNAc or the core 3 disaccharide GlcNAc-(1->3)-beta-GalNAc) [1,2]. The enzyme may play an important role in the degradation and utilization of mucins having core 1 O-glycan.
History
EC 3.2.1.97 created 1978 (EC 3.2.1.110 created 1984, incorporated 2008), modified 2008, modified 2011
Orthology
K17624  
endo-alpha-N-acetylgalactosaminidase
Genes
BCR: 
BCQ: 
BCQ_1996(gcaD)
BNC: 
BTF: 
SSD: 
SDT: 
SPSE_0100(spsG)
SPN: 
SPD: 
SPR: 
SPW: 
SPX: 
SNE: 
SPV: 
SNM: 
SJJ: 
SPP: 
SNT: 
SNC: 
SNB: 
SNP: 
SNI: 
SNV: 
SNX: 
SND: 
SNU: 
SPNG: 
SPNE: 
SPNU: 
SPNM: 
SPNO: 
SPNN: 
SMB: 
SOR: 
EFL: 
EFD: 
EFN: 
MPX: 
APR: 
SCO: 
SCO6348(SC3A7.16c)
SSX: 
SCT: 
SCY: 
SVE: 
SFI: 
SALU: 
ARR: 
PAX: 
KAL: 
BLO: 
BLJ: 
BLD_1258(aprE)
BLF: 
BLB: 
BLM: 
BLK: 
BBI: 
BBP: 
BBF: 
 » show all
Taxonomy
Reference
1  [PMID:18559962]
  Authors
Ashida H, Maki R, Ozawa H, Tani Y, Kiyohara M, Fujita M, Imamura A, Ishida H, Kiso M, Yamamoto K
  Title
Characterization of two different endo-alpha-N-acetylgalactosaminidases from probiotic and pathogenic enterobacteria, Bifidobacterium longum and Clostridium perfringens.
  Journal
Glycobiology. 18 (2008) 727-34.
  Organism
Bifidobacterium longum, Clostridium perfringens
Reference
2  [PMID:18635885]
  Authors
Koutsioulis D, Landry D, Guthrie EP
  Title
Novel endo-alpha-N-acetylgalactosaminidases with broader substrate specificity.
  Journal
Glycobiology. 18 (2008) 799-805.
Reference
3  [PMID:16141207]
  Authors
Fujita K, Oura F, Nagamine N, Katayama T, Hiratake J, Sakata K, Kumagai H, Yamamoto K
  Title
Identification and molecular cloning of a novel glycoside hydrolase family of core 1 type O-glycan-specific endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum.
  Journal
J. Biol. Chem. 280 (2005) 37415-22.
  Organism
Bifidobacterium longum
Reference
4  [PMID:19502354]
  Authors
Suzuki R, Katayama T, Kitaoka M, Kumagai H, Wakagi T, Shoun H, Ashida H, Yamamoto K, Fushinobu S
  Title
Crystallographic and mutational analyses of substrate recognition of endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum.
  Journal
J. Biochem. 146 (2009) 389-98.
  Organism
Bifidobacterium longum
Reference
5  [PMID:19194003]
  Authors
Gregg KJ, Boraston AB
  Title
Cloning, recombinant production, crystallization and preliminary X-ray diffraction analysis of a family 101 glycoside hydrolase from Streptococcus pneumoniae.
  Journal
Acta. Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 65 (2009) 133-5.
Reference
6  [PMID:10620364]
  Authors
Ashida H, Yamamoto K, Murata T, Usui T, Kumagai H
  Title
Characterization of endo-alpha-N-acetylgalactosaminidase from Bacillus sp. and syntheses of neo-oligosaccharides using its transglycosylation activity.
  Journal
Arch. Biochem. Biophys. 373 (2000) 394-400.
Reference
7  [PMID:18725192]
  Authors
Goda HM, Ushigusa K, Ito H, Okino N, Narimatsu H, Ito M
  Title
Molecular cloning, expression, and characterization of a novel endo-alpha-N-acetylgalactosaminidase from Enterococcus faecalis.
  Journal
Biochem. Biophys. Res. Commun. 375 (2008) 441-6.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
59793-96-3

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