D00664
type: Enzyme
rlcp: p994
cath: TIM Barrel
cath: Immunoglobulin-like
ec: https://purl.uniprot.org/enzyme/3.2.1.22
csa: 1uas
uniprot: Q92456
uniprot: Q9FXT4
uniprot: P06280
kegg enzyme: Alpha-galactosidase
kegg pathway: Galactose metabolism
kegg pathway: Glycerolipid metabolism
kegg pathway: Sphingolipid metabolism
kegg pathway: Glycosphingolipid biosynthesis - globoseries
kegg substrate: alpha-D-galactoside
kegg substrate: Melibiose
kegg substrate: galactomannan
kegg substrate: H2O
kegg product: alpha-D-Galactose
kegg product: alpha-D-galactoside
kegg product: D-Glucose
kegg product: 1,4-beta-D-Mannan
kegg intermediate: Peptidyl-ASP-beta-D-galactose
pdb: 1sznA01
pdb: 1t0oA01
pdb: 1uasA01
pdb: 1r46A01
pdb: 1r46B01
pdb: 1r47A01
pdb: 1r47B01
pdb: 3gxnA01
pdb: 3gxnB01
pdb: 3gxpA01
pdb: 3gxpB01
pdb: 3gxtA01
pdb: 3gxtB01
pdb: 3hg2A01
pdb: 3hg2B01
pdb: 3hg3A01
pdb: 3hg3B01
pdb: 3hg4A01
pdb: 3hg4B01
pdb: 3hg5A01
pdb: 3hg5B01
pdb: 1sznA02
pdb: 1t0oA02
pdb: 1uasA02
pdb: 1r46A02
pdb: 1r46B02
pdb: 1r47A02
pdb: 1r47B02
pdb: 3gxnA02
pdb: 3gxnB02
pdb: 3gxpA02
pdb: 3gxpB02
pdb: 3gxtA02
pdb: 3gxtB02
pdb: 3hg2A02
pdb: 3hg2B02
pdb: 3hg3A02
pdb: 3hg3B02
pdb: 3hg4A02
pdb: 3hg4B02
pdb: 3hg5A02
pdb: 3hg5B02
active site residues resources: Crystal structure of rice alpha-galactosidase complexed with D-galactose.
active site residues resources: The molecular defect leading to Fabry disease: structure of human alpha-galactosidase.
active site residues resources: Crystal structure of alpha-galactosidase from Trichoderma reesei and its complex with galactose: implications for catalytic mechanism.
active site residues resources: ¿-Galactosidases and their applications in biotransformations.
active site residues resources: Effects of pH and iminosugar pharmacological chaperones on lysosomal glycosidase structure and stability.
active site residues resources: The tetramer structure of the glycoside hydrolase family 27 alpha-galactosidase I from Umbelopsis vinacea.
active site residues resources: Catalytic mechanism of human alpha-galactosidase.
active site residues resources: P06280
active site residues resources: Q9FXT4
references: Identification of Asp-130 as the catalytic nucleophile in the main alpha-galactosidase from Phanerochaete chrysosporium, a family 27 glycosyl hydrolase.
references: The synthesis, testing and use of 5-fluoro-alpha-D-galactosyl fluoride to trap an intermediate on green coffee bean alpha-galactosidase and identify the catalytic nucleophile.
references: The 1.9 A structure of alpha-N-acetylgalactosaminidase: molecular basis of glycosidase deficiency diseases.
references: Crystal structure of rice alpha-galactosidase complexed with D-galactose.
references: The molecular defect leading to Fabry disease: structure of human alpha-galactosidase.
references: Crystal structure of alpha-galactosidase from Trichoderma reesei and its complex with galactose: implications for catalytic mechanism.

TIM Barrel
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.20.20.70
catalytic domain: index.html

Immunoglobulin-like
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.60.40.1180

Galactose metabolism
type: KeggPathway
references: KEGG:MAP00052

Glycerolipid metabolism
type: KeggPathway
references: KEGG:MAP00561

Sphingolipid metabolism
type: KeggPathway
references: KEGG:MAP00600

Glycosphingolipid biosynthesis - globoseries
type: KeggPathway
references: KEGG:MAP00603

alpha-D-galactoside
type: KeggSubstrate
type: KeggProduct
references: KEGG:L00045
compound type: polysaccharide

Melibiose
type: KeggSubstrate
references: KEGG:C05402
references: CHEBI:28053
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: polysaccharide

galactomannan
type: KeggSubstrate
references: KEGG:C00883
references: CHEBI:27680
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: polysaccharide

H2O
type: KeggSubstrate
references: KEGG:C00001
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: H2O

alpha-D-Galactose
type: KeggProduct
references: KEGG:C00984
references: CHEBI:28061
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: carbohydrate

D-Glucose
type: KeggProduct
references: KEGG:C00031
references: CHEBI:4167
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: carbohydrate

1,4-beta-D-Mannan
type: KeggProduct
references: KEGG:C02492
compound type: polysaccharide

Peptidyl-ASP-beta-D-galactose
type: KeggIntermediate
references: KEGG:I00062

1sznA01
type: Pdb
references: 1szn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1szn
catalytic residue: ASP 54;TYR 96;ASP 132;ARG 222;ASP 226

1t0oA01
type: Pdb
references: 1t0o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t0o
catalytic residue: ASP 54;TYR 96;ASP 132;ARG 222;ASP 226

1uasA01
type: Pdb
references: 1uas
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1uas
catalytic residue: ASP 51;TYR 93;ASP 130;ARG 181;ASP 185

1r46A01
type: Pdb
references: 1r46
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1r46
catalytic residue: ASP 92;TYR 134;ASP 170;ARG 227;ASP 231

1r46B01
type: Pdb
references: 1r46
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1r46
catalytic residue: ASP 92;TYR 134;ASP 170;ARG 227;ASP 231

1r47A01
type: Pdb
references: 1r47
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1r47
catalytic residue: ASP 92;TYR 134;ASP 170;ARG 227;ASP 231

1r47B01
type: Pdb
references: 1r47
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1r47
catalytic residue: ASP 92;TYR 134;ASP 170;ARG 227;ASP 231

3gxnA01
type: Pdb
references: 3gxn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3gxn
catalytic residue: ASP 92;TYR 134;ASP 170;ARG 227;ASP 231

3gxnB01
type: Pdb
references: 3gxn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3gxn
catalytic residue: ASP 92;TYR 134;ASP 170;ARG 227;ASP 231

3gxpA01
type: Pdb
references: 3gxp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3gxp
catalytic residue: ASP 92;TYR 134;ASP 170;ARG 227;ASP 231

3gxpB01
type: Pdb
references: 3gxp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3gxp
catalytic residue: ASP 92;TYR 134;ASP 170;ARG 227;ASP 231

3gxtA01
type: Pdb
references: 3gxt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3gxt
catalytic residue: ASP 92;TYR 134;ASP 170;ARG 227;ASP 231

3gxtB01
type: Pdb
references: 3gxt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3gxt
catalytic residue: ASP 92;TYR 134;ASP 170;ARG 227;ASP 231

3hg2A01
type: Pdb
references: 3hg2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hg2
catalytic residue: ASP 92;TYR 134;ASP 170;ARG 227;ASP 231

3hg2B01
type: Pdb
references: 3hg2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hg2
catalytic residue: ASP 92;TYR 134;ASP 170;ARG 227;ASP 231

3hg3A01
type: Pdb
references: 3hg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hg3
catalytic residue: ASP 92;TYR 134; ;ARG 227;ASP 231
comment: mutant D170A

3hg3B01
type: Pdb
references: 3hg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hg3
catalytic residue: ASP 92;TYR 134; ;ARG 227;ASP 231
comment: mutant D170A

3hg4A01
type: Pdb
references: 3hg4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hg4
catalytic residue: ASP 92;TYR 134;ASP 170;ARG 227;ASP 231

3hg4B01
type: Pdb
references: 3hg4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hg4
catalytic residue: ASP 92;TYR 134;ASP 170;ARG 227;ASP 231

3hg5A01
type: Pdb
references: 3hg5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hg5
catalytic residue: ASP 92;TYR 134;ASP 170;ARG 227;ASP 231

3hg5B01
type: Pdb
references: 3hg5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hg5
catalytic residue: ASP 92;TYR 134;ASP 170;ARG 227;ASP 231

Crystal structure of rice alpha-galactosidase complexed with D-galactose.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 56-417 IN COMPLEX WITH D-GALACTOSE.
references: http://www.ncbi.nlm.nih.gov/pubmed/12657636
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q9FXT4
journal: J Biol Chem
volume: 278
pages: 20313-8
published year: 2003
authors:
  item: Fujimoto Z
  item: Kaneko S
  item: Momma M
  item: Kobayashi H
  item: Mizuno H

The molecular defect leading to Fabry disease: structure of human alpha-galactosidase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 32-422 IN COMPLEX WITH PRODUCT, HOMODIMERIZATION, GLYCOSYLATION AT ASN-139; ASN-192 AND ASN-215.
references: http://www.ncbi.nlm.nih.gov/pubmed/15003450
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P06280
journal: J Mol Biol
volume: 337
pages: 319-35
published year: 2004
authors:
  item: Garman SC
  item: Garboczi DN

Crystal structure of alpha-galactosidase from Trichoderma reesei and its complex with galactose: implications for catalytic mechanism.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 28-441.
references: http://www.ncbi.nlm.nih.gov/pubmed/15136043
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q92456
journal: J Mol Biol
volume: 339
pages: 413-22
published year: 2004
authors:
  item: Golubev AM
  item: Nagem RA
  item: Brandao Neto JR
  item: Neustroev KN
  item: Eneyskaya EV
  item: Kulminskaya AA
  item: Shabalin KA
  item: Savel'ev AN
  item: Polikarpov I

¿-Galactosidases and their applications in biotransformations.
type: BibliographicResource
journal: Biocatal Biotransformation
volume: 27
pages: 79-89
published year: 2009
authors:
  item: Weignerova' L
  item: Simerska' P
  item: Kr(en V

Effects of pH and iminosugar pharmacological chaperones on lysosomal glycosidase structure and stability.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/19374450
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P06280
journal: Biochemistry
volume: 48
pages: 4816-27
published year: 2009
authors:
  item: Lieberman RL
  item: D'aquino JA
  item: Ringe D
  item: Petsko GA

The tetramer structure of the glycoside hydrolase family 27 alpha-galactosidase I from Umbelopsis vinacea.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/19809163
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biosci Biotechnol Biochem
volume: 73
pages: 2360-4
published year: 2009
authors:
  item: Fujimoto Z
  item: Kaneko S
  item: Kim WD
  item: Park GG
  item: Momma M
  item: Kobayashi H

Catalytic mechanism of human alpha-galactosidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/19940122
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P06280
journal: J Biol Chem
volume: 285
pages: 3625-32
published year: 2010
authors:
  item: Guce AI
  item: Clark NE
  item: Salgado EN
  item: Ivanen DR
  item: Kulminskaya AA
  item: Brumer H 3rd
  item: Garman SC

Identification of Asp-130 as the catalytic nucleophile in the main alpha-galactosidase from Phanerochaete chrysosporium, a family 27 glycosyl hydrolase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10933800
journal: Biochemistry
volume: 39
pages: 9826-36
published year: 2000
authors:
  item: Hart DO
  item: He S
  item: Chany CJ 2nd
  item: Withers SG
  item: Sims PF
  item: Sinnott ML
  item: Brumer H 3rd

The synthesis, testing and use of 5-fluoro-alpha-D-galactosyl fluoride to trap an intermediate on green coffee bean alpha-galactosidase and identify the catalytic nucleophile.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11128583
journal: Carbohydr Res
volume: 329
pages: 539-47
published year: 2000
authors:
  item: Ly HD
  item: Howard S
  item: Shum K
  item: He S
  item: Zhu A
  item: Withers SG

The 1.9 A structure of alpha-N-acetylgalactosaminidase: molecular basis of glycosidase deficiency diseases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12005440
journal: Structure
volume: 10
pages: 425-34
published year: 2002
authors:
  item: Garman SC
  item: Hannick L
  item: Zhu A
  item: Garboczi DN

Melibiase
type: KeggEnzyme

Alpha-D-galactosidase
type: KeggEnzyme

Alpha-galactosidase A
type: KeggEnzyme

Alpha-galactoside galactohydrolase
type: KeggEnzyme

Analogue
compound: alpha-D-Galactose
pdb: 1t0oA01
ligand het code: GAL

Analogue
compound: alpha-D-Galactose
pdb: 1r47A01
ligand het code: GAL

Analogue
compound: alpha-D-Galactose
pdb: 1r47B01
ligand het code: GAL

Analogue
compound: alpha-D-Galactose
pdb: 3gxtA01
ligand het code: NOJ

Analogue
compound: alpha-D-Galactose
pdb: 3gxtB01
ligand het code: NOJ

IntermediateAnalogue
compound: Peptidyl-ASP-beta-D-galactose
pdb: 3hg4A01
ligand het code: 7JZ

IntermediateAnalogue
compound: Peptidyl-ASP-beta-D-galactose
pdb: 3hg4B01
ligand het code: 7JZ

ReferenceForCatalyticMechanism
reference index: 3
reference section: Figure 4

ReferenceForCatalyticMechanism
reference index: 6
reference section: p.417-419

ReferenceForCatalyticMechanism
reference index: 9
reference section: FIGURE 1

ReferenceForCatalyticMechanism
reference index: 10
reference section: Fig.2, Fig.3, p.3627-3630