S00391
type: Enzyme
cath: L-fuculose-1-phosphate Aldolase
ec: https://purl.uniprot.org/enzyme/4.1.2.17
csa: 1fua
macie: M0072
uniprot: P0AB87
kegg enzyme: L-fuculose-phosphate aldolase
kegg enzyme: L-fuculose 1-phosphate aldolase
kegg enzyme: fuculose aldolase
kegg enzyme: L-fuculose-1-phosphate lactaldehyde-lyase
kegg pathway: Fructose and mannose metabolism
kegg cofactor: Zinc
kegg substrate: L-Fuculose 1-phosphate
kegg product: Glycerone phosphate
kegg product: (S)-Lactaldehyde
pdb: 1dzuP
pdb: 1dzvP
pdb: 1dzwP
pdb: 1dzxP
pdb: 1dzyP
pdb: 1dzzP
pdb: 1e46P
pdb: 1e47P
pdb: 1e48P
pdb: 1e49P
pdb: 1e4aP
pdb: 1e4bP
pdb: 1e4cP
pdb: 1fuaA
pdb: 2fuaA
pdb: 3fuaA
pdb: 4fuaA
pdb bound state: Unbound
  compound: L-Fuculose 1-phosphate
  pdb: 1dzuP
pdb bound state: Unbound
  compound: L-Fuculose 1-phosphate
  pdb: 1dzvP
pdb bound state: Unbound
  compound: L-Fuculose 1-phosphate
  pdb: 1dzwP
pdb bound state: Unbound
  compound: L-Fuculose 1-phosphate
  pdb: 1dzxP
pdb bound state: Unbound
  compound: L-Fuculose 1-phosphate
  pdb: 1dzyP
pdb bound state: Unbound
  compound: L-Fuculose 1-phosphate
  pdb: 1dzzP
pdb bound state: Unbound
  compound: L-Fuculose 1-phosphate
  pdb: 1e46P
pdb bound state: Unbound
  compound: L-Fuculose 1-phosphate
  pdb: 1e47P
pdb bound state: Unbound
  compound: L-Fuculose 1-phosphate
  pdb: 1e48P
pdb bound state: Unbound
  compound: L-Fuculose 1-phosphate
  pdb: 1e49P
pdb bound state: Unbound
  compound: L-Fuculose 1-phosphate
  pdb: 1e4aP
pdb bound state: Unbound
  compound: L-Fuculose 1-phosphate
  pdb: 1e4bP
pdb bound state: Unbound
  compound: L-Fuculose 1-phosphate
  pdb: 1e4cP
pdb bound state: Unbound
  compound: L-Fuculose 1-phosphate
  pdb: 1fuaA
pdb bound state: Unbound
  compound: L-Fuculose 1-phosphate
  pdb: 2fuaA
pdb bound state: Unbound
  compound: L-Fuculose 1-phosphate
  pdb: 3fuaA
pdb bound state: Unbound
  compound: L-Fuculose 1-phosphate
  pdb: 4fuaA
pdb bound state: Analogue
  compound: Zinc
  pdb: 2fuaA
  ligand het code: _CO
pdb bound state: Unbound
  compound: Glycerone phosphate
  pdb: 1dzuP
pdb bound state: Unbound
  compound: Glycerone phosphate
  pdb: 1dzvP
pdb bound state: Unbound
  compound: Glycerone phosphate
  pdb: 1dzwP
pdb bound state: Unbound
  compound: Glycerone phosphate
  pdb: 1dzxP
pdb bound state: Unbound
  compound: Glycerone phosphate
  pdb: 1dzyP
pdb bound state: Unbound
  compound: Glycerone phosphate
  pdb: 1dzzP
pdb bound state: Unbound
  compound: Glycerone phosphate
  pdb: 1e46P
pdb bound state: Unbound
  compound: Glycerone phosphate
  pdb: 1e49P
pdb bound state: Unbound
  compound: Glycerone phosphate
  pdb: 1e4aP
pdb bound state: Unbound
  compound: Glycerone phosphate
  pdb: 1e4bP
pdb bound state: Unbound
  compound: Glycerone phosphate
  pdb: 1e4cP
pdb bound state: Unbound
  compound: Glycerone phosphate
  pdb: 1fuaA
pdb bound state: Unbound
  compound: Glycerone phosphate
  pdb: 2fuaA
pdb bound state: Unbound
  compound: Glycerone phosphate
  pdb: 3fuaA
pdb bound state: Analogue
  compound: Glycerone phosphate
  pdb: 4fuaA
  ligand het code: PGH
pdb bound state: Unbound
  compound: (S)-Lactaldehyde
  pdb: 1dzuP
pdb bound state: Unbound
  compound: (S)-Lactaldehyde
  pdb: 1dzvP
active site residues resources: Epimerization via carbon-carbon bond cleavage. L-ribulose-5-phosphate 4-epimerase as a masked class II aldolase.
active site residues resources: 13C and deuterium isotope effects suggest an aldol cleavage mechanism for L-ribulose-5-phosphate 4-epimerase.
active site residues resources: P0AB87
references: The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli.
references: Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli.
references: Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure.
references: Epimerization via carbon-carbon bond cleavage. L-ribulose-5-phosphate 4-epimerase as a masked class II aldolase.
references: Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis.
references: 13C and deuterium isotope effects suggest an aldol cleavage mechanism for L-ribulose-5-phosphate 4-epimerase.
references: Structures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis.
references: The structure of L-ribulose-5-phosphate 4-epimerase: an aldolase-like platform for epimerization.
references: Catalysis and binding in L-ribulose-5-phosphate 4-epimerase: a comparison with L-fuculose-1-phosphate aldolase.
comment: This enzyme belongs to the aldolase class II family, which utilizes the metal ion as cofactor.

L-fuculose-1-phosphate Aldolase
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.225.10
catalytic domain: index.html

Fructose and mannose metabolism
type: KeggPathway
references: KEGG:MAP00051

Zinc
type: KeggCofactor
references: KEGG:C00038
compound type: heavy metal
references: CHEBI:29105
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

L-Fuculose 1-phosphate
type: KeggSubstrate
references: KEGG:C01099
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: CHEBI:16647
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Glycerone phosphate
type: KeggProduct
references: KEGG:C00111
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: CHEBI:16108
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

(S)-Lactaldehyde
type: KeggProduct
references: KEGG:C00424
compound type: carbohydrate
references: CHEBI:18041
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1dzuP
type: Pdb
references: 1dzu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dzu
catalytic residue: GLU 73;TYR 113
cofactor binding residue: GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
comment: mutant T26A

1dzvP
type: Pdb
references: 1dzv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dzv
catalytic residue: GLU 73;
cofactor binding residue: GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
comment: mutant Y113F;Y209F

1dzwP
type: Pdb
references: 1dzw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dzw
catalytic residue: GLU 73;TYR 113
cofactor binding residue: GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
comment: mutant F131A

1dzxP
type: Pdb
references: 1dzx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dzx
catalytic residue: GLU 73;TYR 113
cofactor binding residue: GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
comment: mutant R212A

1dzyP
type: Pdb
references: 1dzy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dzy
catalytic residue: GLU 73;TYR 113
cofactor binding residue: GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
comment: mutant E214A

1dzzP
type: Pdb
references: 1dzz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dzz
catalytic residue: GLU 73;
cofactor binding residue: GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
comment: mutant Y113F

1e46P
type: Pdb
references: 1e46
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e46
catalytic residue: ;TYR 113
cofactor binding residue: ;HIS 92;HIS 94;HIS 155(Zinc binding)
comment: mutant E73S

1e47P
type: Pdb
references: 1e47
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e47
catalytic residue: ;TYR 113
cofactor binding residue: ;HIS 92;HIS 94;HIS 155(Zinc binding)
comment: mutant E73Q

1e48P
type: Pdb
references: 1e48
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e48
catalytic residue: ;
cofactor binding residue: ;HIS 92;HIS 94;HIS 155(Zinc binding)
comment: mutant E73Q;Y113F;Y209F

1e49P
type: Pdb
references: 1e49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e49
catalytic residue: GLU 73;TYR 113
cofactor binding residue: GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
comment: mutant N29L;S71A

1e4aP
type: Pdb
references: 1e4a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e4a
catalytic residue: GLU 73;TYR 113
cofactor binding residue: GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
comment: deletion A27

1e4bP
type: Pdb
references: 1e4b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e4b
catalytic residue: GLU 73;TYR 113
cofactor binding residue: GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
comment: mutant N29Q

1e4cP
type: Pdb
references: 1e4c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e4c
catalytic residue: GLU 73;TYR 113
cofactor binding residue: GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
comment: mutant S71Q

1fuaA
type: Pdb
references: 1fua
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fua
catalytic residue: GLU 73;TYR 113
cofactor binding residue: GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)

2fuaA
type: Pdb
references: 2fua
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2fua
catalytic residue: GLU 73;TYR 113
cofactor binding residue: GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)

3fuaA
type: Pdb
references: 3fua
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3fua
catalytic residue: GLU 73;TYR 113
cofactor binding residue: GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)

4fuaA
type: Pdb
references: 4fua
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4fua
catalytic residue: GLU 73;TYR 113
cofactor binding residue: GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)

The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8515438
journal: J Mol Biol
volume: 231
pages: 549-53
published year: 1993
authors:
  item: Dreyer MK
  item: Schulz GE

Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
journal: Acta Crystallogr D Biol Crystallogr
volume: 52
pages: 1082-91
published year: 1996
authors:
  item: Dreyer MK
  item: Schulz GE
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0AB87

Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND CATALYTIC MECHANISM.
medline id: 96256522
references: http://www.ncbi.nlm.nih.gov/pubmed/8676381
journal: J Mol Biol
volume: 259
pages: 458-66
published year: 1996
authors:
  item: Dreyer MK
  item: Schulz GE
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0AB87

Epimerization via carbon-carbon bond cleavage. L-ribulose-5-phosphate 4-epimerase as a masked class II aldolase.
type: BibliographicResource
comment: Homologous enzyme
references: http://www.ncbi.nlm.nih.gov/pubmed/9548961
journal: Biochemistry
volume: 37
pages: 5746-54
published year: 1998
authors:
  item: Johnson AE
  item: Tanner ME

Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS), AND MUTAGENESIS.
medline id: 20281325
references: http://www.ncbi.nlm.nih.gov/pubmed/10821675
journal: Biochemistry
volume: 39
pages: 6033-41
published year: 2000
authors:
  item: Joerger AC
  item: Gosse C
  item: Fessner WD
  item: Schulz GE
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0AB87

13C and deuterium isotope effects suggest an aldol cleavage mechanism for L-ribulose-5-phosphate 4-epimerase.
type: BibliographicResource
comment: Homologous enzyme
references: http://www.ncbi.nlm.nih.gov/pubmed/10769138
journal: Biochemistry
volume: 39
pages: 4808-20
published year: 2000
authors:
  item: Lee LV
  item: Vu MV
  item: Cleland WW

Structures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY OF MUTANTS.
medline id: 20510153
references: http://www.ncbi.nlm.nih.gov/pubmed/11054289
journal: J Mol Biol
volume: 303
pages: 531-43
published year: 2000
authors:
  item: Joerger AC
  item: Mueller-Dieckmann C
  item: Schulz GE
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0AB87

The structure of L-ribulose-5-phosphate 4-epimerase: an aldolase-like platform for epimerization.
type: BibliographicResource
comment: Homologous enzyme
references: http://www.ncbi.nlm.nih.gov/pubmed/11732895
journal: Biochemistry
volume: 40
pages: 14763-71
published year: 2001
authors:
  item: Luo Y
  item: Samuel J
  item: Mosimann SC
  item: Lee JE
  item: Tanner ME
  item: Strynadka NC

Catalysis and binding in L-ribulose-5-phosphate 4-epimerase: a comparison with L-fuculose-1-phosphate aldolase.
type: BibliographicResource
comment: Homologous enzyme
references: http://www.ncbi.nlm.nih.gov/pubmed/11732896
journal: Biochemistry
volume: 40
pages: 14772-80
published year: 2001
authors:
  item: Samuel J
  item: Luo Y
  item: Morgan PM
  item: Strynadka NC
  item: Tanner ME

ReferenceForCatalyticMechanism
reference index: 3
reference section: Fig.6, p.463-465
reference step: 3

ReferenceForCatalyticMechanism
reference index: 4
reference section: Fig.6, p.5752
reference step: 2

ReferenceForCatalyticMechanism
reference index: 5
reference section: Fig.3

ReferenceForCatalyticMechanism
reference index: 8
reference section: Fig.2

ReferenceForCatalyticMechanism
reference index: 9
reference section: Fig.1