KEGG   ENZYME: 3.2.1.97
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
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)
R04527 R06140(G)
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
BCRBCAH187_A2112 BCAH187_A2113
BCQBCQ_1996(gcaD)
BNCBCN_1925 BCN_1926
BTFYBT020_10440 YBT020_10445
BPACLMD38_16550
BPANNLJ82_09930
BACAFAY30_22180
CSOALIS82_04775
VHLBME96_15600
VIGBKP57_16755
VILCFK37_08520
VPNA21D_00287
VPTKBP50_13210
LEXLen3610_12745
NMKCHR53_24360
NCMQNK12_27450
BVJI5776_03565
SSDSPSINT_2361
SDTSPSE_0100(spsG)
SDPNCTC12225_00120(spsG)
SSCHLH95_00870
SSCZRN70_01085
SLZB5P37_05525
SFQC7J90_02955
SSCUCEP64_07700
SSTESAMEA4384403_1657(spsG)
PAEFR50345_08715
PAEJH70737_09395
PLUTEI981_04495
PALBEJC50_09170
PRZGZH47_21840 GZH47_23530
PSPNL1F29_15605
SPNSP_0368
SPDSPD_0335
SPRspr0328
SPWSPCG_0364
SJJSPJ_0354
SNVSPNINV200_03290
SPXSPG_0333
SNTSPT_0411
SNDMYY_0445
SPNNT308_01820
SNESPN23F03400
SPVSPH_0475
SNCHMPREF0837_10665
SNMSP70585_0439
SPPSPP_0406
SNIINV104_03160
SPNGHMPREF1038_00418
SNBSP670_0436
SNPSPAP_0392
SNXSPNOXC03640
SNUSPNA45_01682
SPNESPN034156_14200
SPNUSPN034183_03700
SPNMSPN994038_03580
SPNOSPN994039_03590
SMBsmi_1538
SORSOR_1643
STVV470_08050
STRNSNAG_1587
SGWD7D53_00665
SLATJ4854_09260
SACOSAME_00232
EFAEF1800
EFLEF62_2171
EFIOG1RF_11509
EFDEFD32_1530
EFSEFS1_1608
EFNDENG_01981
EFQDR75_793
MPXMPD5_0190
ASANAWM72_00235
ADCFOC79_05010
GSGCYJ72_009755
FCTNRE15_06530
GADK8O88_01435
CPECPE0693
CPFCPF_0685
CCHVBTM20_02260 BTM20_04415 BTM20_05745
CSEPCP523_01860 CP523_03285
CGASJ1C67_08575
BHANCGC63_05270
RLRNQ541_03490
VGUHYG85_01730 HYG85_07490 HYG85_14120
APRApre_1674
AVGI6H45_08395
ERIEEI45_06575
ERDG7062_02345
EIOH9L01_04840
AARGAargi30884_10080 Aargi30884_22190
ABSIA9CBEGH2_11290 A9CBEGH2_19980
SMOERGT18_19620
EHNH9Q80_12365
CSTCLK434_10115
SCOSCO6348(SC3A7.16c)
SGRSGR_1945
SGBWQO_25750
SFISFUL_5426
SANLKZO11_27305
SCYER2B67_08515
SSXSACTE_4756
SVESVEN_5220
SALSSLNWT_5875
SLVSLIV_06420
SVTSVTN_26820
STREGZL_06509
SLDT261_6164
SLCSL103_09225
SPRISPRI_2326
SCZABE83_09575
STRTA8713_30835
SCLFBB341_22020
SALWCP975_08750
SNRSNOUR_30295
SALUDC74_2489
SALLSAZ_13790
STRDNI25_36400
SSIAA7J05_26805
SVUB1H20_26300
SGVB1H19_11975
SALFSMD44_02207(engBF)
SALJSMD11_5036(engBF)
STROSTRMOE7_10845
SFKKY5_1983c
SLKSLUN_28070
SKACP970_32660
SVNCP980_04270
SRKFGW37_08410
SFICEIZ62_08730
SCAVCVT27_25145
SBYH7H31_27460
SRIMCP984_30925
SCINCP977_24510
SGXH4W23_28335
SSPBCP982_11865
SPLACP981_09945
SATAC5746_04820 C5746_29505
SDWK7C20_09480
SCALI6J39_25980
SAUHSU9_007925
SPEUCGZ69_25705
SXNIAG42_10035 IAG42_26735
SHKJ2N69_08575
SANUK7396_26895
STRYEQG64_26170
SINEKI385_12630
SAOVG3H79_28095
SDURM4V62_31080
STAALDH80_12575
SNIGHEK616_14930
STUBMMF93_07940
SXTKPP03845_106656
SLONLGI35_30390
SDRZNEH16_08830
STUDSTRTU_005394
SENGOJ254_18055
SYUNMOV08_30315
SOVQZH56_27320
SFIYF0344_09110
SHAUK9S39_33020
SLAIP8A22_02540 P8A22_10755
SFPQUY26_30115
SCTSCAT_1146
SCYSCATT_11440
KABB7C62_27050
MIPAXH82_08770
MOYCVS54_00552
MLIQNMQ05_02075
MPAOIZR02_02065
MRGSM116_02735
MESTPTQ19_14630
ARRARUE_c13800
ARWMB46_03125
ARNCGK93_07595
AWWG8758_02045
ARIUM93_08010
AAUAAur_1465
PNVJMY29_06865
PSEYGU243_11900
BRXBH708_10990
BRVCFK39_08600
BRZCFK38_02185
LMOIVV02_02330
OEKFFI11_002435
PACPPA1569
PAKHMPREF0675_4636
PAVTIA2EST22_07865
PAXTIA2EST36_07845
PAZTIA2EST2_07775
PAWPAZ_c16570
PADTIIST44_00840
PACCPAC1_08245
CACNRN83_08300
PRLBCB70_10565
CEQUO6R08_07175
KQIF1D05_28745
KSLOG809_20780
NOABKM31_27850
NGNLCN96_18690
AABA4R43_09090
KALKALB_2141
ACTUActkin_04202
CROSN8J89_23455
SNASnas_1136
AHEArch_1772
TPYOX956_07740
TPECHLG82_06990
TBERQPC17_06525
ACTOC3V41_03525
AIRNCTC12972_00812
AWEJG540_05130
AVUBK816_01970
GHMCJ187_002530
BLOBL0464
BLJBLD_1258(aprE)
BLFBLIF_0157
BLBBBMN68_1202(aprE)
BLMBLLJ_0168
BLKBLNIAS_02561
BLZBLGT_01150
BBPBBPR_0264
BBIBBIF_0285
BBFBBB_0248
BGXESN35_08770
BLEMBL8807_07765
BEUBE0216_03280
ALUSSTSP2_01314 STSP2_02214 STSP2_02710
PGSCPT03_12230
 » show all
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 18:727-34 (2008)
DOI:10.1093/glycob/cwn053
  Sequence
[cpe:CPE0693]
Reference
2  [PMID:18635885]
  Authors
Koutsioulis D, Landry D, Guthrie EP
  Title
Novel endo-alpha-N-acetylgalactosaminidases with broader substrate specificity.
  Journal
Glycobiology 18:799-805 (2008)
DOI:10.1093/glycob/cwn069
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 280:37415-22 (2005)
DOI:10.1074/jbc.M506874200
  Sequence
[blm:BLLJ_0168]
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 146:389-98 (2009)
DOI:10.1093/jb/mvp086
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 65:133-5 (2009)
DOI:10.1107/S1744309108042474
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 373:394-400 (2000)
DOI:10.1006/abbi.1999.1565
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 375:441-6 (2008)
DOI:10.1016/j.bbrc.2008.08.065
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 3.2.1.97
IUBMB Enzyme Nomenclature: 3.2.1.97
ExPASy - ENZYME nomenclature database: 3.2.1.97
BRENDA, the Enzyme Database: 3.2.1.97
CAS: 59793-96-3

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