D00017
type: Enzyme
cath: Rossmann fold
cath: Dihydrodipicolinate Reductase; domain 2
ec: https://purl.uniprot.org/enzyme/1.1.99.28
csa: 1ofg
uniprot: Q07982
kegg enzyme: glucose-fructose oxidoreductase
kegg cofactor: NADPH
kegg substrate: D-Glucose
kegg substrate: D-Fructose
kegg product: D-Gluconolactone
kegg product: D-Sorbitol
pdb: 1ofgA01
pdb: 1ofgB01
pdb: 1ofgC01
pdb: 1ofgD01
pdb: 1ofgE01
pdb: 1ofgF01
pdb: 1evjA01
pdb: 1evjB01
pdb: 1evjC01
pdb: 1evjD01
pdb: 1h6aA01
pdb: 1h6aB01
pdb: 1h6bA01
pdb: 1h6bB01
pdb: 1h6cA01
pdb: 1h6cB01
pdb: 1h6dA01
pdb: 1h6dB01
pdb: 1h6dC01
pdb: 1h6dD01
pdb: 1h6dE01
pdb: 1h6dF01
pdb: 1h6dG01
pdb: 1h6dH01
pdb: 1h6dI01
pdb: 1h6dJ01
pdb: 1h6dK01
pdb: 1h6dL01
pdb: 1ofgA02
pdb: 1ofgB02
pdb: 1ofgC02
pdb: 1ofgD02
pdb: 1ofgE02
pdb: 1ofgF02
pdb: 1evjA02
pdb: 1evjB02
pdb: 1evjC02
pdb: 1evjD02
pdb: 1h6aA02
pdb: 1h6aB02
pdb: 1h6bA02
pdb: 1h6bB02
pdb: 1h6cA02
pdb: 1h6cB02
pdb: 1h6dA02
pdb: 1h6dB02
pdb: 1h6dC02
pdb: 1h6dD02
pdb: 1h6dE02
pdb: 1h6dF02
pdb: 1h6dG02
pdb: 1h6dH02
pdb: 1h6dI02
pdb: 1h6dJ02
pdb: 1h6dK02
pdb: 1h6dL02
pdb bound state: Unbound
  compound: D-Glucose
  pdb: 1ofgA01
pdb bound state: Unbound
  compound: D-Glucose
  pdb: 1ofgB01
pdb bound state: Unbound
  compound: D-Glucose
  pdb: 1ofgC01
pdb bound state: Unbound
  compound: D-Glucose
  pdb: 1ofgD01
active site residues resources: A multistep process is responsible for product-induced inactivation of glucose-fructose oxidoreductase from Zymomonas mobilis.
references: Crystallization and preliminary X-ray analysis of glucose-fructose oxidoreductase from Zymomonas mobilis.
references: The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP.
references: A multistep process is responsible for product-induced inactivation of glucose-fructose oxidoreductase from Zymomonas mobilis.
references: Roles of His-79 and Tyr-180 of D-xylose/dihydrodiol dehydrogenase in catalytic function.
references: Crystal structure of a truncated mutant of glucose-fructose oxidoreductase shows that an N-terminal arm controls tetramer formation.
references: Crystal structures of the precursor form of glucose-fructose oxidoreductase from Zymomonas mobilis and its complexes with bound ligands.
references: Galactosyl-mimodye ligands for Pseudomonas fluorescens beta-galactose dehydrogenase.

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.720
catalytic domain: index.html

Dihydrodipicolinate Reductase; domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.360.10
catalytic domain: index.html

NADPH
type: KeggCofactor
references: KEGG:C00005
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:16474
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

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

D-Fructose
type: KeggSubstrate
references: KEGG:C10906
compound type: carbohydrate
references: CHEBI:48095
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

D-Gluconolactone
type: KeggProduct
references: KEGG:C00198
compound type: carbohydrate
references: CHEBI:16217
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

D-Sorbitol
type: KeggProduct
references: KEGG:C00794
compound type: carbohydrate
references: CHEBI:17924
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1ofgA01
type: Pdb
references: 1ofg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ofg
catalytic residue: LYS 129

1ofgB01
type: Pdb
references: 1ofg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ofg
catalytic residue: LYS 129

1ofgC01
type: Pdb
references: 1ofg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ofg
catalytic residue: LYS 129

1ofgD01
type: Pdb
references: 1ofg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ofg
catalytic residue: LYS 129

1ofgE01
type: Pdb
references: 1ofg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ofg
catalytic residue: LYS 129

1ofgF01
type: Pdb
references: 1ofg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ofg
catalytic residue: LYS 129

1evjA01
type: Pdb
references: 1evj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evj
catalytic residue: LYS 129

1evjB01
type: Pdb
references: 1evj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evj
catalytic residue: LYS 129

1evjC01
type: Pdb
references: 1evj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evj
catalytic residue: LYS 129

1evjD01
type: Pdb
references: 1evj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evj
catalytic residue: LYS 129

1h6aA01
type: Pdb
references: 1h6a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6a
catalytic residue: LYS 181

1h6aB01
type: Pdb
references: 1h6a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6a
catalytic residue: LYS 181

1h6bA01
type: Pdb
references: 1h6b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6b
catalytic residue: LYS 181

1h6bB01
type: Pdb
references: 1h6b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6b
catalytic residue: LYS 181

1h6cA01
type: Pdb
references: 1h6c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6c
catalytic residue: LYS 181

1h6cB01
type: Pdb
references: 1h6c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6c
catalytic residue: LYS 181

1h6dA01
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: LYS 181

1h6dB01
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: LYS 181

1h6dC01
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: LYS 181

1h6dD01
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: LYS 181

1h6dE01
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: LYS 181

1h6dF01
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: LYS 181

1h6dG01
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: LYS 181

1h6dH01
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: LYS 181

1h6dI01
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: LYS 181

1h6dJ01
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: LYS 181

1h6dK01
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: LYS 181

1h6dL01
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: LYS 181

1ofgA02
type: Pdb
references: 1ofg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ofg
catalytic residue: TYR 217

1ofgB02
type: Pdb
references: 1ofg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ofg
catalytic residue: TYR 217

1ofgC02
type: Pdb
references: 1ofg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ofg
catalytic residue: TYR 217

1ofgD02
type: Pdb
references: 1ofg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ofg
catalytic residue: TYR 217

1ofgE02
type: Pdb
references: 1ofg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ofg
catalytic residue: TYR 217

1ofgF02
type: Pdb
references: 1ofg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ofg
catalytic residue: TYR 217

1evjA02
type: Pdb
references: 1evj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evj
catalytic residue: TYR 217

1evjB02
type: Pdb
references: 1evj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evj
catalytic residue: TYR 217

1evjC02
type: Pdb
references: 1evj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evj
catalytic residue: TYR 217

1evjD02
type: Pdb
references: 1evj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evj
catalytic residue: TYR 217

1h6aA02
type: Pdb
references: 1h6a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6a
catalytic residue: TYR 269

1h6aB02
type: Pdb
references: 1h6a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6a
catalytic residue: TYR 269

1h6bA02
type: Pdb
references: 1h6b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6b
catalytic residue: TYR 269

1h6bB02
type: Pdb
references: 1h6b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6b
catalytic residue: TYR 269

1h6cA02
type: Pdb
references: 1h6c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6c
catalytic residue: TYR 269

1h6cB02
type: Pdb
references: 1h6c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6c
catalytic residue: TYR 269

1h6dA02
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: TYR 269

1h6dB02
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: TYR 269

1h6dC02
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: TYR 269

1h6dD02
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: TYR 269

1h6dE02
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: TYR 269

1h6dF02
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: TYR 269

1h6dG02
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: TYR 269

1h6dH02
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: TYR 269

1h6dI02
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: TYR 269

1h6dJ02
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: TYR 269

1h6dK02
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: TYR 269

1h6dL02
type: Pdb
references: 1h6d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h6d
catalytic residue: TYR 269

Crystallization and preliminary X-ray analysis of glucose-fructose oxidoreductase from Zymomonas mobilis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7756998
journal: Protein Sci
volume: 3
pages: 2447-9
published year: 1994
authors:
  item: Loos H
  item: Ermler U
  item: Sprenger GA
  item: Sahm H

The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)
medline id: 97148336
references: http://www.ncbi.nlm.nih.gov/pubmed/8994968
journal: Structure
volume: 4
pages: 1413-28
published year: 1996
authors:
  item: Kingston RL
  item: Scopes RK
  item: Baker EN
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q07982

A multistep process is responsible for product-induced inactivation of glucose-fructose oxidoreductase from Zymomonas mobilis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9490072
journal: Eur J Biochem
volume: 251
pages: 955-63
published year: 1998
authors:
  item: Furlinger M
  item: Haltrich D
  item: Kulbe KD
  item: Nidetzky B

Roles of His-79 and Tyr-180 of D-xylose/dihydrodiol dehydrogenase in catalytic function.
type: BibliographicResource
comment: D00017-15
references: http://www.ncbi.nlm.nih.gov/pubmed/11097839
journal: Biochem Biophys Res Commun
volume: 278
pages: 333-7
published year: 2000
authors:
  item: Asada Y
  item: Aoki S
  item: Ishikura S
  item: Usami N
  item: Hara A

Crystal structure of a truncated mutant of glucose-fructose oxidoreductase shows that an N-terminal arm controls tetramer formation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11099381
journal: J Mol Biol
volume: 304
pages: 575-84
published year: 2000
authors:
  item: Lott JS
  item: Halbig D
  item: Baker HM
  item: Hardman MJ
  item: Sprenger GA
  item: Baker EN
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structures of the precursor form of glucose-fructose oxidoreductase from Zymomonas mobilis and its complexes with bound ligands.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11705375
journal: Biochemistry
volume: 40
pages: 13857-67
published year: 2001
authors:
  item: Nurizzo D
  item: Halbig D
  item: Sprenger GA
  item: Baker EN
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Galactosyl-mimodye ligands for Pseudomonas fluorescens beta-galactose dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12423337
journal: Eur J Biochem
volume: 269
pages: 5391-405
published year: 2002
authors:
  item: Mazitsos CF
  item: Rigden DJ
  item: Tsoungas PG
  item: Clonis YD

Analogue
compound: D-Glucose
pdb: 1h6bA02
ligand het code: GOL

Analogue
compound: D-Glucose
pdb: 1h6bB02
ligand het code: GOL

Analogue
compound: D-Glucose
pdb: 1h6dA02
ligand het code: GOL

Analogue
compound: D-Glucose
pdb: 1h6dB02
ligand het code: GOL

Analogue
compound: D-Glucose
pdb: 1h6dC02
ligand het code: GOL

Analogue
compound: D-Glucose
pdb: 1h6dD02
ligand het code: GOL

Analogue
compound: D-Glucose
pdb: 1h6dE02
ligand het code: GOL

Analogue
compound: D-Glucose
pdb: 1h6dF02
ligand het code: GOL

Analogue
compound: D-Glucose
pdb: 1h6dG02
ligand het code: GOL

Analogue
compound: D-Glucose
pdb: 1h6dH02
ligand het code: GOL

Analogue
compound: D-Glucose
pdb: 1h6dI02
ligand het code: GOL

Analogue
compound: D-Glucose
pdb: 1h6dJ02
ligand het code: GOL

Analogue
compound: D-Glucose
pdb: 1h6dK02
ligand het code: GOL

Analogue
compound: D-Glucose
pdb: 1h6dL02
ligand het code: GOL

Analogue
compound: NADPH
pdb: 1evjA01
ligand het code: NAD

Analogue
compound: NADPH
pdb: 1evjB01
ligand het code: NAD

Analogue
compound: NADPH
pdb: 1evjC01
ligand het code: NAD

Analogue
compound: NADPH
pdb: 1evjD01
ligand het code: NAD

ReferenceForCatalyticMechanism
reference index: 2
reference section: p.1420-1422

ReferenceForCatalyticMechanism
reference index: 6
reference section: p.13865-13866