S00199
type: Enzyme
rlcp: p113
rlcp: p6111
rlcp: p6580
cath: TIM Barrel
ec: https://purl.uniprot.org/enzyme/4.1.2.13
csa: 1ald
uniprot: P04075
uniprot: P05062
uniprot: P00883
uniprot: P07764
uniprot: P14223
uniprot: P07752
kegg enzyme: fructose-bisphosphate aldolase
kegg pathway: Glycolysis / Gluconeogenesis
kegg pathway: Pentose phosphate pathway
kegg pathway: Fructose and mannose metabolism
kegg pathway: Carbon fixation in photosynthetic organisms
kegg substrate: D-Fructose 1,6-bisphosphate
kegg product: Glycerone phosphate
kegg product: D-Glyceraldehyde 3-phosphate
pdb: 1a5cA
pdb: 1a5cB
pdb: 1adoA
pdb: 1adoB
pdb: 1adoC
pdb: 1adoD
pdb: 1aldA
pdb: 1epxA
pdb: 1epxB
pdb: 1epxC
pdb: 1epxD
pdb: 1ewdA
pdb: 1ewdB
pdb: 1ewdC
pdb: 1ewdD
pdb: 1eweA
pdb: 1eweB
pdb: 1eweC
pdb: 1eweD
pdb: 1ewgA
pdb: 1ewgB
pdb: 1ewgC
pdb: 1ewgD
pdb: 1ex5A
pdb: 1ex5B
pdb: 1ex5C
pdb: 1ex5D
pdb: 1f2jA
pdb: 1fbaA
pdb: 1fbaB
pdb: 1fbaC
pdb: 1fbaD
pdb: 1j4eA
pdb: 1j4eB
pdb: 1j4eC
pdb: 1j4eD
pdb: 1qo5A
pdb: 1qo5B
pdb: 1qo5C
pdb: 1qo5D
pdb: 1qo5E
pdb: 1qo5F
pdb: 1qo5G
pdb: 1qo5H
pdb: 1qo5I
pdb: 1qo5J
pdb: 1qo5K
pdb: 1qo5L
pdb: 1qo5M
pdb: 1qo5N
pdb: 1qo5O
pdb: 1qo5P
pdb: 1qo5Q
pdb: 1qo5R
pdb: 2aldA
pdb: 4aldA
pdb: 6aldA
pdb: 6aldB
pdb: 6aldC

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

Glycolysis / Gluconeogenesis
type: KeggPathway
references: KEGG:MAP00010

Pentose phosphate pathway
type: KeggPathway
references: KEGG:MAP00030

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

Carbon fixation in photosynthetic organisms
type: KeggPathway
references: KEGG:MAP00710

D-Fructose 1,6-bisphosphate
type: KeggSubstrate
references: KEGG:C00354
references: CHEBI:37736
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: carbohydrate
compound type: phosphate group/phosphate ion

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

D-Glyceraldehyde 3-phosphate
type: KeggProduct
references: KEGG:C00118
references: CHEBI:29052
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: carbohydrate
compound type: phosphate group/phosphate ion

1a5cA
type: Pdb
references: 1a5c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5c
catalytic residue: ASP 39;LYS 151;GLU 194;GLU 196;LYS 236

1a5cB
type: Pdb
references: 1a5c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5c
catalytic residue: ASP 39;LYS 151;GLU 194;GLU 196;LYS 236

1adoA
type: Pdb
references: 1ado
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ado
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1adoB
type: Pdb
references: 1ado
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ado
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1adoC
type: Pdb
references: 1ado
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ado
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1adoD
type: Pdb
references: 1ado
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ado
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1aldA
type: Pdb
references: 1ald
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ald
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1epxA
type: Pdb
references: 1epx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epx
catalytic residue: ASP 43;LYS 156;GLU 197;GLU 199;LYS 239

1epxB
type: Pdb
references: 1epx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epx
catalytic residue: ASP 43;LYS 156;GLU 197;GLU 199;LYS 239

1epxC
type: Pdb
references: 1epx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epx
catalytic residue: ASP 43;LYS 156;GLU 197;GLU 199;LYS 239

1epxD
type: Pdb
references: 1epx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epx
catalytic residue: ASP 43;LYS 156;GLU 197;GLU 199;LYS 239

1ewdA
type: Pdb
references: 1ewd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ewd
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1ewdB
type: Pdb
references: 1ewd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ewd
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1ewdC
type: Pdb
references: 1ewd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ewd
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1ewdD
type: Pdb
references: 1ewd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ewd
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1eweA
type: Pdb
references: 1ewe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ewe
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;
comment: mutant K229M

1eweB
type: Pdb
references: 1ewe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ewe
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;
comment: mutant K229M

1eweC
type: Pdb
references: 1ewe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ewe
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;
comment: mutant K229M

1eweD
type: Pdb
references: 1ewe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ewe
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;
comment: mutant K229M

1ewgA
type: Pdb
references: 1ewg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ewg
catalytic residue: ASP 33;LYS 146; ;GLU 189;LYS 229
comment: mutant E187Q

1ewgB
type: Pdb
references: 1ewg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ewg
catalytic residue: ASP 33;LYS 146; ;GLU 189;LYS 229
comment: mutant E187Q

1ewgC
type: Pdb
references: 1ewg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ewg
catalytic residue: ASP 33;LYS 146; ;GLU 189;LYS 229
comment: mutant E187Q

1ewgD
type: Pdb
references: 1ewg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ewg
catalytic residue: ASP 33;LYS 146; ;GLU 189;LYS 229
comment: mutant E187Q

1ex5A
type: Pdb
references: 1ex5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ex5
catalytic residue: ASP 33;LYS 146; ;GLU 189;LYS 229
comment: mutant E187A

1ex5B
type: Pdb
references: 1ex5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ex5
catalytic residue: ASP 33;LYS 146; ;GLU 189;LYS 229
comment: mutant E187A

1ex5C
type: Pdb
references: 1ex5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ex5
catalytic residue: ASP 33;LYS 146; ;GLU 189;LYS 229
comment: mutant E187A

1ex5D
type: Pdb
references: 1ex5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ex5
catalytic residue: ASP 33;LYS 146; ;GLU 189;LYS 229
comment: mutant E187A

1f2jA
type: Pdb
references: 1f2j
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f2j
catalytic residue: ASP 43;LYS 156;GLU 197;GLU 199;LYS 239

1fbaA
type: Pdb
references: 1fba
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fba
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1fbaB
type: Pdb
references: 1fba
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fba
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1fbaC
type: Pdb
references: 1fba
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fba
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1fbaD
type: Pdb
references: 1fba
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fba
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1j4eA
type: Pdb
references: 1j4e
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j4e
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1j4eB
type: Pdb
references: 1j4e
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j4e
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1j4eC
type: Pdb
references: 1j4e
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j4e
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1j4eD
type: Pdb
references: 1j4e
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j4e
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5A
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5B
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5C
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5D
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5E
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5F
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5G
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5H
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5I
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5J
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5K
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5L
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5M
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5N
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5O
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5P
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5Q
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

1qo5R
type: Pdb
references: 1qo5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qo5
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

2aldA
type: Pdb
references: 2ald
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ald
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

4aldA
type: Pdb
references: 4ald
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4ald
catalytic residue: ASP 33;LYS 146;GLU 187;GLU 189;LYS 229

6aldA
type: Pdb
references: 6ald
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6ald
catalytic residue: ASP 33; ;GLU 187;GLU 189;LYS 229
comment: mutant K146A

6aldB
type: Pdb
references: 6ald
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6ald
catalytic residue: ASP 33; ;GLU 187;GLU 189;LYS 229
comment: mutant K146A

6aldC
type: Pdb
references: 6ald
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6ald
catalytic residue: ASP 33; ;GLU 187;GLU 189;LYS 229
comment: mutant K146A

6aldD
type: Pdb
references: 6ald
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6ald
catalytic residue: ASP 33; ;GLU 187;GLU 189;LYS 229
comment: mutant K146A

IntermediateBound
pdb: 1j4eA
ligand het code: 13P

IntermediateBound
pdb: 1j4eB
ligand het code: 13P

IntermediateBound
pdb: 1j4eC
ligand het code: 13P

IntermediateBound
pdb: 1j4eD
ligand het code: 13P

Brownian dynamics simulations of aldolase binding glyceraldehyde 3-phosphate dehydrogenase and the possibility of substrate channeling.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11371431
journal: Biophys J
volume: 80
pages: 2527-35
published year: 2001
authors:
  item: Ouporov IV
  item: Knull HR
  item: Huber A
  item: Thomasson KA

Docking multiple conformations of a flexible ligand into a protein binding site using NMR restraints.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11835505
journal: Proteins
volume: 46
pages: 295-307
published year: 2002
authors:
  item: Zabell AP
  item: Post CB

ReferenceForCatalyticMechanism
reference index: 11
reference section: SCHEME 3, p.135-136

ReferenceForCatalyticMechanism
reference index: 16
reference section: SCHEME 1

ReferenceForCatalyticMechanism
reference index: 26
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 32
reference section: Scheme 2

ReferenceForCatalyticMechanism
reference index: 33
reference section: Fig.2, Fig.3, p.38-39
reference step: 6

ReferenceForCatalyticMechanism
reference index: 34
reference section: Scheme 1, p.12294, p.12996-12997
reference step: 5

ReferenceForCatalyticMechanism
reference index: 40
reference section: p.36-38

ReferenceForCatalyticMechanism
reference index: 41
reference section: Scheme 1, p.2088-2089
reference step: 6

ReferenceForCatalyticMechanism
reference index: 43
reference section: p.12662-12663

ReferenceForCatalyticMechanism
reference index: 45
reference section: p.295, Table 3

ReferenceForCatalyticMechanism
reference index: 46
reference section: p.823

ReferenceForCatalyticMechanism
reference index: 47
reference section: p.1149-1150

ReferenceForCatalyticMechanism
reference index: 51
reference section: Fig.5, p.13874
reference step: 10

ReferenceForCatalyticMechanism
reference index: 54
reference section: p.9482

Alternative binding of two sequential glycolytic enzymes to microtubules. Molecular studies in the phosphofructokinase/aldolase/microtubule system.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9325270
journal: J Biol Chem
volume: 272
pages: 25542-6
published year: 1997
authors:
  item: Vertessy BG
  item: Orosz F
  item: Kovacs J
  item: Ovadi J

Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
medline id: 97143309
references: http://www.ncbi.nlm.nih.gov/pubmed/8989320
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00883
journal: Nat Struct Biol
volume: 4
pages: 36-9
published year: 1997
authors:
  item: Blom N
  item: Sygusch J

18O studies of the mechanisms of yeast and muscle aldolases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/4607364
journal: Biochemistry
volume: 13
pages: 4371-5
published year: 1974
authors:
  item: Heron EJ
  item: Caprioli RM

Proton exchange of the pro-S hydrogen at C-1 in dihydroxyacetone phosphate, D-fructose 1,6-bisphosphate and D-fructose 1-phosphate catalysed by rabbit-muscle aldolase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/954748
journal: Eur J Biochem
volume: 66
pages: 95-104
published year: 1976
authors:
  item: Lowe G
  item: Pratt RF

Affinity labeling of a previously undetected essential lysyl residue in class I fructose bisphosphate aldolase.
type: BibliographicResource
comment: ACTIVE SITE.
medline id: 76190154
references: http://www.ncbi.nlm.nih.gov/pubmed/5453
references: P00883
journal: J Biol Chem
volume: 251
pages: 3057-62
published year: 1976
authors:
  item: Hartman FC
  item: Brown JP

Rabbit muscle aldolase catalyzed proton exchange of hydroxyacetone phosphate with solvent.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/911752
journal: Biochemistry
volume: 16
pages: 3988-94
published year: 1977
authors:
  item: Pratt RF

Interaction of the aldolase and the membrane of human erythrocytes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/18166
journal: Biochemistry
volume: 16
pages: 2966-71
published year: 1977
authors:
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  item: Steck TL

Changes associated with glycolytic-enzyme binding in the equatorial X-ray-diffraction pattern of glycerinated rabbit psoas muscle.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/540038
journal: Biochem J
volume: 183
pages: 663-7
published year: 1979
authors:
  item: Stewart M
  item: Morton DJ
  item: Clarke FM

Identification of the C-1-phosphate-binding arginine residue of rabbit-muscle aldolase. Isolation of 1,2-cyclohexanedione-labeled peptide by chemisorption chromatography.
type: BibliographicResource
comment: SUBSTRATE-BINDING SITE.
medline id: 80046697
references: http://www.ncbi.nlm.nih.gov/pubmed/499203
references: P00883
journal: Eur J Biochem
volume: 99
pages: 309-13
published year: 1979
authors:
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  item: Varadi A
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  item: Kovacs K

Changes in activity of fructose-1,6-bisphosphate aldolase in livers of fasted rabbits and accumulation of crossreacting immune material.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/293723
journal: Proc Natl Acad Sci U S A
volume: 76
pages: 6323-5
published year: 1979
authors:
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Membrane-bound fructose 1,6-bisphosphate aldolase: catalytic activity and mechanisms of desorption.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7385224
journal: Tohoku J Exp Med
volume: 130
pages: 143-52
published year: 1980
authors:
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The low-resolution structure of human muscle aldolase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6115420
journal: Philos Trans R Soc Lond B Biol Sci
volume: 293
pages: 209-14
published year: 1981
authors:
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Chemistry of proton abstraction by glycolytic enzymes (aldolase, isomerases and pyruvate kinase).
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6115413
journal: Philos Trans R Soc Lond B Biol Sci
volume: 293
pages: 131-43
published year: 1981
authors:
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A 1H n.m.r. study of isotope exchange catalysed by glycolytic enzymes in the human erythrocyte.
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references: http://www.ncbi.nlm.nih.gov/pubmed/7092833
journal: Biochem J
volume: 202
pages: 589-602
published year: 1982
authors:
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Fructose-1,6-bisphosphate-aldolase from rabbit muscle. Half of the sites reactivity at low temperature.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6838539
journal: Biochem Biophys Res Commun
volume: 110
pages: 578-83
published year: 1983
authors:
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Mechanism of aldolase binding to erythrocyte membrane: Part II. Kinetic aspects.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6679317
journal: Biochem Int
volume: 6
pages: 53-61
published year: 1983
authors:
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Interaction of the dissociable glycerol-3-phosphate dehydrogenase and fructose-1,6-bisphosphate aldolase. Quantitative analysis by an extrinsic fluorescence probe.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6406231
journal: Eur J Biochem
volume: 133
pages: 433-7
published year: 1983
authors:
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Fructose-1,6-bisphosphate aldolase from rabbit muscle: different catalytic behavior of the dihydroxyacetone phosphate binding sites at low temperature.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6486803
journal: Arch Biochem Biophys
volume: 233
pages: 595-602
published year: 1984
authors:
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Extreme X-ray sensitive modification of type I aldolases by blue dye ligand chromatography.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6487321
journal: Biochem Biophys Res Commun
volume: 123
pages: 1069-75
published year: 1984
authors:
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Characterization and comparison of soluble and immobilized pig muscle aldolases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/4026283
journal: Appl Biochem Biotechnol
volume: 11
pages: 91-100
published year: 1985
authors:
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Structure of rabbit muscle aldolase at low resolution.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/4066671
journal: J Biol Chem
volume: 260
pages: 15286-90
published year: 1985
authors:
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Specific, limited tryptic modification of wheat-germ fructose-bisphosphate aldolase subunits: destruction of catalytic activity but not of ability to establish precise subunit-subunit recognition.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3942758
journal: Biochim Biophys Acta
volume: 869
pages: 185-91
published year: 1986
authors:
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A simple approach to detect active-site-directed enzyme-enzyme interactions. The aldolase/glycerol-phosphate-dehydrogenase enzyme system.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3569280
journal: Eur J Biochem
volume: 164
pages: 655-9
published year: 1987
authors:
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Human aldolase A deficiency associated with a hemolytic anemia: thermolabile aldolase due to a single base mutation.
type: BibliographicResource
comment: VARIANT HEMOLYTIC ANEMIA GLY-128.
medline id: 88068641
references: http://www.ncbi.nlm.nih.gov/pubmed/2825199
references: P04075
journal: Proc Natl Acad Sci U S A
volume: 84
pages: 8623-7
published year: 1987
authors:
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Immobilization of pig muscle aldolase on a silica-based support.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2556962
journal: Appl Biochem Biotechnol
volume: 22
pages: 223-35
published year: 1989
authors:
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The crystal structure of human muscle aldolase at 3.0 A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
medline id: 90242948
references: http://www.ncbi.nlm.nih.gov/pubmed/2335208
references: P04075
journal: FEBS Lett
volume: 262
pages: 282-6
published year: 1990
authors:
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Human aldolase A of a hemolytic anemia patient with Asp-128----Gly substitution: characteristics of an enzyme generated in E. coli transfected with the expression plasmid pHAAD128G.
type: BibliographicResource
comment: VARIANT HEMOLYTIC ANEMIA GLY-128.
medline id: 91035340
references: http://www.ncbi.nlm.nih.gov/pubmed/2229018
references: P04075
journal: J Biochem (Tokyo)
volume: 108
pages: 153-7
published year: 1990
authors:
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Topography and conformational changes of fructose-1,6-bisphosphate aldolase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1814134
journal: Acta Biochim Pol
volume: 38
pages: 407-21
published year: 1991
authors:
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The crystal structure of fructose-1,6-bisphosphate aldolase from Drosophila melanogaster at 2.5 A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
medline id: 92070498
references: http://www.ncbi.nlm.nih.gov/pubmed/1959612
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P07764
journal: FEBS Lett
volume: 292
pages: 237-42
published year: 1991
authors:
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Carboxyl terminus region modulates catalytic activity of recombinant maize aldolase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1894606
journal: J Biol Chem
volume: 266
pages: 17099-105
published year: 1991
authors:
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Activity and specificity of human aldolases.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
medline id: 91278081
references: http://www.ncbi.nlm.nih.gov/pubmed/2056525
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references: P04075
journal: J Mol Biol
volume: 219
pages: 573-6
published year: 1991
authors:
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Metabolite channeling versus free diffusion: reinterpretation of aldolase-catalysed inactivation of glyceraldehyde-3-phosphate dehydrogenase.
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references: http://www.ncbi.nlm.nih.gov/pubmed/1417758
journal: Biochem J
volume: 286
pages: 977-9
published year: 1992
authors:
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Aldolase-catalyzed diketone phosphate formation from oxoaldehydes. NMR studies and metabolic significance.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1577806
journal: J Biol Chem
volume: 267
pages: 9713-7
published year: 1992
authors:
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Paracatalytic self-inactivation of fructose-1,6-bisphosphate aldolase. Structure of the crosslink formed at the active site.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8513801
journal: Eur J Biochem
volume: 214
pages: 515-9
published year: 1993
authors:
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A data-based reaction mechanism for type I fructose bisphosphate aldolase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8488556
journal: Trends Biochem Sci
volume: 18
pages: 36-9
published year: 1993
authors:
  item: Littlechild JA
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Lysine-146 of rabbit muscle aldolase is essential for cleavage and condensation of the C3-C4 bond of fructose 1,6-bis(phosphate).
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7918450
journal: Biochemistry
volume: 33
pages: 12291-7
published year: 1994
authors:
  item: Morris AJ
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Solution structure of a band 3 peptide inhibitor bound to aldolase: a proposed mechanism for regulating binding by tyrosine phosphorylation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8527430
journal: Biochemistry
volume: 34
pages: 16574-84
published year: 1995
authors:
  item: Schneider ML
  item: Post CB

The molecular nature of the F-actin binding activity of aldolase revealed with site-directed mutants.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8636111
journal: J Biol Chem
volume: 271
pages: 6861-5
published year: 1996
authors:
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Disruption of the aldolase A tetramer into catalytically active monomers.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8643582
journal: Proc Natl Acad Sci U S A
volume: 93
pages: 5374-9
published year: 1996
authors:
  item: Beernink PT
  item: Tolan DR

Crystallisation and Preliminary X-Ray Diffraction Studies on Human Liver Aldolase.
type: BibliographicResource
comment: X-ray crystallography
journal: Protein Pept Lett
volume: 3
pages: 207-12
published year: 1996
authors:
  item: Dalby A
  item: Rawas A
  item: Watson HC
  item: Littlechild JA
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Immune versus natural selection: antibody aldolases with enzymic rates but broader scope.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9405338
journal: Science
volume: 278
pages: 2085-92
published year: 1997
authors:
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  item: Zhong G
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  item: List B
  item: Anderson J
  item: Stura EA
  item: Wilson IA
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Crystal structure of fructose-1,6-bisphosphate aldolase from the human malaria parasite Plasmodium falciparum.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
medline id: 98190013
references: http://www.ncbi.nlm.nih.gov/pubmed/9521758
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P14223
journal: Biochemistry
volume: 37
pages: 4388-96
published year: 1998
authors:
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Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its natural substrate in a cleavage-defective mutant at 2.3 A(,).
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10504235
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biochemistry
volume: 38
pages: 12655-64
published year: 1999
authors:
  item: Choi KH
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  item: Morris AJ
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  item: Tolan DR
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Mechanism of metabolite transfer in coupled two-enzyme reactions involving aldolase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10336621
journal: Eur J Biochem
volume: 262
pages: 371-6
published year: 1999
authors:
  item: Pettersson H
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Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
medline id: 99156067
references: http://www.ncbi.nlm.nih.gov/pubmed/10048322
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P04075
journal: Protein Sci
volume: 8
pages: 291-7
published year: 1999
authors:
  item: Dalby A
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  item: Littlechild JA

Functional and molecular modelling studies of two hereditary fructose intolerance-causing mutations at arginine 303 in human liver aldolase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10970798
journal: Biochem J
volume: 350 Pt 3
pages: 823-8
published year: 2000
authors:
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  item: Zancan L
  item: Zagari A
  item: Salvatore F

Expression, purification, and characterization of natural mutants of human aldolase B. Role of quaternary structure in catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10625657
journal: J Biol Chem
volume: 275
pages: 1145-51
published year: 2000
authors:
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Structures of type 2 peroxisomal targeting signals in two trypanosomatid aldolases.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10891264
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references: P07752
journal: J Mol Biol
volume: 300
pages: 697-707
published year: 2000
authors:
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Chemoenzymatic synthesis of the microbial elicitor (-)-syringolide via a fructose 1,6-diphosphate aldolase-catalyzed condensation reaction.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10959854
journal: J Org Chem
volume: 65
pages: 4529-31
published year: 2000
authors:
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The structure of human liver fructose-1,6-bisphosphate aldolase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
references: http://www.ncbi.nlm.nih.gov/pubmed/11679716
references: P05062
journal: Acta Crystallogr D Biol Crystallogr
volume: 57
pages: 1526-33
published year: 2001
authors:
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Snapshots of catalysis: the structure of fructose-1,6-(bis)phosphate aldolase covalently bound to the substrate dihydroxyacetone phosphate.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11705376
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biochemistry
volume: 40
pages: 13868-75
published year: 2001
authors:
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  item: Shi J
  item: Hopkins CE
  item: Tolan DR
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Structural and functional analysis of aldolase B mutants related to hereditary fructose intolerance.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12417303
journal: FEBS Lett
volume: 531
pages: 152-6
published year: 2002
authors:
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  item: Viola A
  item: Zagari A
  item: Salvatore F

A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11779856
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Biol Chem
volume: 277
pages: 9474-83
published year: 2002
authors:
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  item: Sygusch J

Presteady-state kinetic evidence for a ring-opening activity in fructose-1,6-(bis)phosphate aldolase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15025449
journal: J Am Chem Soc
volume: 126
pages: 3402-3
published year: 2004
authors:
  item: Choi KH
  item: Tolan DR

aldolase
type: KeggEnzyme

fructose-1,6-bisphosphate triosephosphate-lyase
type: KeggEnzyme

fructose diphosphate aldolase
type: KeggEnzyme

diphosphofructose aldolase
type: KeggEnzyme

fructose 1,6-diphosphate aldolase
type: KeggEnzyme

ketose 1-phosphate aldolase
type: KeggEnzyme

phosphofructoaldolase
type: KeggEnzyme

zymohexase
type: KeggEnzyme

fructoaldolase
type: KeggEnzyme

fructose 1-phosphate aldolase
type: KeggEnzyme

fructose 1-monophosphate aldolase
type: KeggEnzyme

1,6-Diphosphofructose aldolase
type: KeggEnzyme

SMALDO
type: KeggEnzyme

D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase
type: KeggEnzyme