T00086
type: Enzyme
cath: Fumarase C; Chain B, domain 1
cath: Fumarase C; Chain A, domain 2
cath: Ribonucleotide Reductase Protein R1; domain 1
ec: https://purl.uniprot.org/enzyme/4.2.1.2
csa: 1fuq
uniprot: P05042
uniprot: O66271
uniprot: P08417
kegg enzyme: fumarate hydratase
kegg pathway: Citrate cycle (TCA cycle)
kegg pathway: Reductive carboxylate cycle (CO2 fixation)
kegg substrate: (S)-Malate
kegg product: Fumarate
kegg product: H2O
pdb: 1fuoA01
pdb: 1fuoB01
pdb: 1fupA01
pdb: 1fupB01
pdb: 1fuqA01
pdb: 1fuqB01
pdb: 1furA01
pdb: 1furB01
pdb: 1kq7A01
pdb: 1kq7B01
pdb: 1yfeA01
pdb: 2fusA01
pdb: 2fusB01
pdb: 1vdkA01
pdb: 1vdkB01
pdb: 1yfmA01
pdb: 1fuoA02
pdb: 1fuoB02
pdb: 1fupA02
pdb: 1fupB02
pdb: 1fuqA02
pdb: 1fuqB02
pdb: 1furA02
pdb: 1furB02
pdb: 1kq7A02
pdb: 1kq7B02
pdb: 1yfeA02
pdb: 2fusA02
pdb: 2fusB02
pdb: 1vdkA02
pdb: 1vdkB02
pdb: 1yfmA02
pdb: 1fuoA03
pdb: 1fuoB03
pdb: 1fupA03
pdb: 1fupB03
pdb: 1fuqA03
pdb: 1fuqB03
pdb: 1furA03
pdb: 1furB03
pdb: 1kq7A03
pdb: 1kq7B03
pdb: 1yfeA03
pdb: 2fusA03
pdb: 2fusB03
pdb: 1vdkA03
pdb: 1vdkB03
pdb: 1yfmA03
active site residues resources: P05042
active site residues resources: P08417
references: Enzyme catalysis: conflicting requirements of substrate access and transition state affinity.
references: The fumarase reaction.
references: Physicochemical, catalytic, and immunochemical properties of fumarases crystallized separately from mitochondrial and cytosolic fractions of rat liver.
references: Spin ECHO proton NMR studies of the metabolism of malate and fumarate in human erythrocytes. Dependence on free NAD levels.
references: Purification, crystallization, and preliminary X-ray data for porcine fumarase.
references: Proton transfer in catalysis by fumarase.
references: Purification, characterization and preliminary X-ray study of fumarase from Saccharomyces cerevisiae.
references: Purification and crystallization of fumarase C from Escherichia coli.
references: Kinetics of enzymes with iso-mechanisms: dead-end inhibition of fumarase and carbonic anhydrase II.
references: The multisubunit active site of fumarase C from Escherichia coli.
references: Importance of historical contingency in the stereochemistry of hydratase-dehydratase enzymes.
references: Purification and characterization of fumarase from the syntrophic propionate-oxidizing bacterium strain MPOB.
references: Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli.
references: Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site.
references: Pig heart fumarase contains two distinct substrate-binding sites differing in affinity.

Fumarase C; Chain B, domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.275.10

Fumarase C; Chain A, domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.20.200.10
catalytic domain: index.html

Ribonucleotide Reductase Protein R1; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.40.30

Citrate cycle (TCA cycle)
type: KeggPathway
references: KEGG:MAP00020

Reductive carboxylate cycle (CO2 fixation)
type: KeggPathway
references: KEGG:MAP00720

(S)-Malate
type: KeggSubstrate
references: KEGG:C00149
compound type: carbohydrate
compound type: carboxyl group
references: CHEBI:30797
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Fumarate
type: KeggProduct
references: KEGG:C00122
compound type: carboxyl group
references: CHEBI:18012
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

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

2fusA01
type: Pdb
references: 2fus
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2fus
comment: mutant H129N

2fusB01
type: Pdb
references: 2fus
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2fus
comment: mutant H129N

1fuoA02
type: Pdb
references: 1fuo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fuo
catalytic residue: HIS 188;SER 318;LYS 324;GLU 331

1fuoB02
type: Pdb
references: 1fuo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fuo
catalytic residue: HIS 188; ;LYS 324;GLU 331
comment: invisible 317-320

1fupA02
type: Pdb
references: 1fup
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fup
catalytic residue: HIS 188;SER 318;LYS 324;GLU 331

1fupB02
type: Pdb
references: 1fup
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fup
catalytic residue: HIS 188; ;LYS 324;GLU 331
comment: invisible 317-320

1fuqA02
type: Pdb
references: 1fuq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fuq
catalytic residue: HIS 188;SER 318;LYS 324;GLU 331

1fuqB02
type: Pdb
references: 1fuq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fuq
catalytic residue: HIS 188; ;LYS 324;GLU 331
comment: invisible 317-320

1furA02
type: Pdb
references: 1fur
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fur
catalytic residue: ;SER 318;LYS 324;GLU 331
comment: mutant H188N

1furB02
type: Pdb
references: 1fur
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fur
catalytic residue: ; ;LYS 324;GLU 331
comment: mutant H188N, invisible 317-320

1kq7A02
type: Pdb
references: 1kq7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kq7
catalytic residue: HIS 188;SER 318;LYS 324;GLU 331
comment: mutant E315Q

1kq7B02
type: Pdb
references: 1kq7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kq7
catalytic residue: HIS 188; ;LYS 324;GLU 331
comment: mutant E315Q, invisible 317-320

1yfeA02
type: Pdb
references: 1yfe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yfe
catalytic residue: HIS 188;SER 318;LYS 324;GLU 331

2fusA02
type: Pdb
references: 2fus
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2fus
catalytic residue: HIS 188;SER 318;LYS 324;GLU 331

2fusB02
type: Pdb
references: 2fus
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2fus
catalytic residue: HIS 188; ;LYS 324;GLU 331
comment: invisible 317-320

1vdkA02
type: Pdb
references: 1vdk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vdk
catalytic residue: HIS 188;SER 318;LYS 324;GLU 331

1vdkB02
type: Pdb
references: 1vdk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vdk
catalytic residue: HIS 188; ;LYS 324;GLU 331
comment: invisible 317-320

1yfmA02
type: Pdb
references: 1yfm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yfm
catalytic residue: HIS 213;SER 343;LYS 349;GLU 356
comment: mutant K289R

Enzyme catalysis: conflicting requirements of substrate access and transition state affinity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/4365214
journal: Mol Cell Biochem
volume: 3
pages: 207-11
published year: 1974
authors:
  item: Wolfenden R

The fumarase reaction.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/893568
journal: J Chem Educ
volume: 54
pages: 515-6
published year: 1977
authors:
  item: Kasperek GJ
  item: Pratt RF

Physicochemical, catalytic, and immunochemical properties of fumarases crystallized separately from mitochondrial and cytosolic fractions of rat liver.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7287666
journal: J Biochem (Tokyo)
volume: 89
pages: 1923-31
published year: 1981
authors:
  item: Kobayashi K
  item: Yamanishi T
  item: Tuboi S

Spin ECHO proton NMR studies of the metabolism of malate and fumarate in human erythrocytes. Dependence on free NAD levels.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7138916
journal: Biochim Biophys Acta
volume: 721
pages: 191-200
published year: 1982
authors:
  item: Simpson RJ
  item: Brindle KM
  item: Campbell ID

Purification, crystallization, and preliminary X-ray data for porcine fumarase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3771571
journal: J Biol Chem
volume: 261
pages: 15183-5
published year: 1986
authors:
  item: Sacchettini JC
  item: Meininger T
  item: Roderick S
  item: Banaszak LJ

Proton transfer in catalysis by fumarase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1327137
journal: Biochemistry
volume: 31
pages: 9993-9
published year: 1992
authors:
  item: Rose IA
  item: Warms JV
  item: Kuo DJ

Purification, characterization and preliminary X-ray study of fumarase from Saccharomyces cerevisiae.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1633200
journal: Biochim Biophys Acta
volume: 1122
pages: 85-92
published year: 1992
authors:
  item: Keruchenko JS
  item: Keruchenko ID
  item: Gladilin KL
  item: Zaitsev VN
  item: Chirgadze NY

Purification and crystallization of fumarase C from Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8496960
journal: J Mol Biol
volume: 231
pages: 141-4
published year: 1993
authors:
  item: Weaver TM
  item: Levitt DG
  item: Banaszak LJ

Kinetics of enzymes with iso-mechanisms: dead-end inhibition of fumarase and carbonic anhydrase II.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8031132
journal: Arch Biochem Biophys
volume: 312
pages: 227-33
published year: 1994
authors:
  item: Rebholz KL
  item: Northrop DB

The multisubunit active site of fumarase C from Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7552727
journal: Nat Struct Biol
volume: 2
pages: 654-62
published year: 1995
authors:
  item: Weaver TM
  item: Levitt DG
  item: Donnelly MI
  item: Stevens PP
  item: Banaszak LJ

Importance of historical contingency in the stereochemistry of hydratase-dehydratase enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7624773
journal: Science
volume: 269
pages: 527-9
published year: 1995
authors:
  item: Mohrig JR
  item: Moerke KA
  item: Cloutier DL
  item: Lane BD
  item: Person EC
  item: Onasch TB

Purification and characterization of fumarase from the syntrophic propionate-oxidizing bacterium strain MPOB.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8593099
journal: Arch Microbiol
volume: 165
pages: 126-31
published year: 1996
authors:
  item: Van Kuijk BL
  item: Van Loo ND
  item: Arendsen AF
  item: Hagen WR
  item: Stams AJ

Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
medline id: 97065812
references: http://www.ncbi.nlm.nih.gov/pubmed/8909293
journal: Biochemistry
volume: 35
pages: 13955-65
published year: 1996
authors:
  item: Weaver T
  item: Banaszak L
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P05042

Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
medline id: 97253450
references: http://www.ncbi.nlm.nih.gov/pubmed/9098893
journal: Protein Sci
volume: 6
pages: 834-42
published year: 1997
authors:
  item: Weaver T
  item: Lees M
  item: Banaszak L
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P05042

Pig heart fumarase contains two distinct substrate-binding sites differing in affinity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9822627
journal: J Biol Chem
volume: 273
pages: 31661-9
published year: 1998
authors:
  item: Beeckmans S
  item: Van Driessche E

Crystal structures of native and recombinant yeast fumarase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
medline id: 98332745
references: http://www.ncbi.nlm.nih.gov/pubmed/9665847
journal: J Mol Biol
volume: 280
pages: 431-42
published year: 1998
authors:
  item: Weaver T
  item: Lees M
  item: Zaitsev V
  item: Zaitseva I
  item: Duke E
  item: Lindley P
  item: McSweeny S
  item: Svensson A
  item: Keruchenko J
  item: Keruchenko I
  item: Gladilin K
  item: Banaszak L
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P08417

The pi-helix translates structure into function.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10739264
journal: Protein Sci
volume: 9
pages: 201-6
published year: 2000
authors:
  item: Weaver TM

Conversion of fumaric acid to L-malic by sol-gel immobilized Saccharomyces cerevisiae in a supported liquid membrane bioreactor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12052057
journal: Biotechnol Prog
volume: 18
pages: 445-50
published year: 2002
authors:
  item: Bressler E
  item: Pines O
  item: Goldberg I
  item: Braun S

X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12021453
journal: Protein Sci
volume: 11
pages: 1552-7
published year: 2002
authors:
  item: Estevez M
  item: Skarda J
  item: Spencer J
  item: Banaszak L
  item: Weaver TM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The role of the allosteric B site in the fumarase reaction.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14990798
journal: Proc Natl Acad Sci U S A
volume: 101
pages: 3393-7
published year: 2004
authors:
  item: Rose IA
  item: Weaver TM

Structure of free fumarase C from Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16204892
journal: Acta Crystallogr D Biol Crystallogr
volume: 61
pages: 1395-401
published year: 2005
authors:
  item: Weaver T
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

fumarase
type: KeggEnzyme

L-malate hydro-lyase
type: KeggEnzyme

(S)-malate hydro-lyase
type: KeggEnzyme

Analogue
compound: (S)-Malate
pdb: 1fuoA01
ligand het code: CIT

Analogue
compound: (S)-Malate
pdb: 1fuoB01
ligand het code: CIT

Analogue
compound: (S)-Malate
pdb: 1fuqA01
ligand het code: CIT

Analogue
compound: (S)-Malate
pdb: 1fuqB01
ligand het code: CIT

Analogue
compound: (S)-Malate
pdb: 1kq7A01
ligand het code: CIT

Analogue
compound: (S)-Malate
pdb: 1kq7B01
ligand het code: CIT

Analogue
compound: (S)-Malate
pdb: 2fusA01
ligand het code: CIT

Analogue
compound: (S)-Malate
pdb: 2fusB01
ligand het code: CIT

ReferenceForCatalyticMechanism
reference index: 10
reference section: Fig.1, p.660-661
reference step: 2

ReferenceForCatalyticMechanism
reference index: 13

ReferenceForCatalyticMechanism
reference index: 16
reference section: p.437-438

ReferenceForCatalyticMechanism
reference index: 20

ReferenceForCatalyticMechanism
reference index: 21
reference section: p.1399