S00221
type: Enzyme
cath: TIM Barrel
ec: https://purl.uniprot.org/enzyme/4.1.1.23
csa: 1dbt
csa: 1eix
macie: M0050
uniprot: O26232
uniprot: P03962
uniprot: P25971
uniprot: P08244
kegg enzyme: orotidine-5'-phosphate decarboxylase
kegg pathway: Pyrimidine metabolism
kegg substrate: Orotidine 5'-phosphate
kegg product: UMP
kegg product: CO2
pdb: 1dbtA
pdb: 1dbtB
pdb: 1dbtC
pdb: 1dqwA
pdb: 1dqwB
pdb: 1dqwC
pdb: 1dqwD
pdb: 1dqxA
pdb: 1dqxB
pdb: 1dqxC
pdb: 1dqxD
pdb: 1dv7A
pdb: 1dvjA
pdb: 1dvjB
pdb: 1dvjC
pdb: 1dvjD
pdb: 1eixA
pdb: 1eixB
pdb: 1eixC
pdb: 1eixD
pdb: 1jjkA
pdb: 1jjkB
pdb: 1jjkC
pdb: 1jjkD
pdb: 1jjkE
pdb: 1jjkF
pdb: 1jjkG
pdb: 1jjkH
pdb: 1jjkI
pdb: 1jjkJ
pdb: 1jjkK
pdb: 1jjkL
pdb: 1jjkM
pdb: 1jjkN
pdb: 1jjkO
pdb: 1jjkP
pdb: 1l2uA
pdb: 1l2uB
active site residues resources: O26232
active site residues resources: P03962
active site residues resources: P25971
references: Dependence of the catalytic activities on the aggregation and conformation states of uridine 5'-phosphate synthase.
references: Dependence of the aggregation and conformation states of uridine 5'-phosphate synthase on pyrimidine nucleotides. Evidence for a regulatory site.
references: Orotidine-5'-monophosphate decarboxylase catalysis: kinetic isotope effects and the state of hybridization of a bound transition-state analogue.
references: Crystallization of yeast orotidine 5'-monophosphate decarboxylase complexed with 1-(5'-phospho-beta-D-ribofuranosyl) barbituric acid.
references: Orotidylate decarboxylase: insights into the catalytic mechanism from substrate specificity studies.
references: A unique catalytic and inhibitor-binding role for Lys93 of yeast orotidylate decarboxylase.
references: Orotidylate decarboxylase of yeast and man.
references: Intrinsic activity and stability of bifunctional human UMP synthase and its two separate catalytic domains, orotate phosphoribosyltransferase and orotidine-5'-phosphate decarboxylase.
references: A proficient enzyme revisited: the predicted mechanism for orotidine monophosphate decarboxylase.
references: No metal cofactor in orotidine 5'-monophosphate decarboxylase.
references: Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5'-monophosphate decarboxylase.
references: Contribution of enzyme-phosphoribosyl contacts to catalysis by orotidine 5'-phosphate decarboxylase.
references: Yeast orotidine-5'-phosphate decarboxylase: steady-state and pre-steady-state analysis of the kinetic mechanism of substrate decarboxylation.
references: Determination of the mechanism of orotidine 5'-monophosphate decarboxylase by isotope effects.
references: Remarkable rate enhancement of orotidine 5'-monophosphate decarboxylase is due to transition-state stabilization rather than to ground-state destabilization.
references: The structural basis for the remarkable catalytic proficiency of orotidine 5'-monophosphate decarboxylase.
references: The crystal structure and mechanism of orotidine 5'-monophosphate decarboxylase.
references: Anatomy of a proficient enzyme: the structure of orotidine 5'-monophosphate decarboxylase in the presence and absence of a potential transition state analog.
references: Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase.
references: Selenomethionine substitution of orotidine-5'-monophosphate decarboxylase causes a change in crystal contacts and space group.
references: Role of enzyme-ribofuranosyl contacts in the ground state and transition state for orotidine 5'-phosphate decarboxylase: a role for substrate destabilization?
references: A reexamination of the substrate utilization of 2-thioorotidine-5'-monophosphate by yeast orotidine-5'-monophosphate decarboxylase.
references: Crystal structures of orotidine monophosphate decarboxylase: does the structure reveal the mechanism of nature's most proficient enzyme?
references: An alternative explanation for the catalytic proficiency of orotidine 5'-phosphate decarboxylase.

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

Pyrimidine metabolism
type: KeggPathway
references: KEGG:MAP00240

Orotidine 5'-phosphate
type: KeggSubstrate
references: KEGG:C01103
compound type: amide group
compound type: carbohydrate
compound type: nucleotide
references: CHEBI:15842
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

UMP
type: KeggProduct
references: KEGG:C00105
compound type: amide group
compound type: nucleotide
references: CHEBI:16695
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

CO2
type: KeggProduct
references: KEGG:C00011
compound type: others
references: CHEBI:16526
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1dbtA
type: Pdb
references: 1dbt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dbt
catalytic residue: LYS 62

1dbtB
type: Pdb
references: 1dbt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dbt
catalytic residue: LYS 62

1dbtC
type: Pdb
references: 1dbt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dbt
catalytic residue: LYS 62

1dqwA
type: Pdb
references: 1dqw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dqw
catalytic residue: LYS 93

1dqwB
type: Pdb
references: 1dqw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dqw
catalytic residue: LYS 93

1dqwC
type: Pdb
references: 1dqw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dqw
catalytic residue: LYS 93

1dqwD
type: Pdb
references: 1dqw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dqw
catalytic residue: LYS 93

1dqxA
type: Pdb
references: 1dqx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dqx
catalytic residue: LYS 93

1dqxB
type: Pdb
references: 1dqx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dqx
catalytic residue: LYS 93

1dqxC
type: Pdb
references: 1dqx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dqx
catalytic residue: LYS 93

1dqxD
type: Pdb
references: 1dqx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dqx
catalytic residue: LYS 93

1dv7A
type: Pdb
references: 1dv7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dv7
catalytic residue: LYS 72

1dvjA
type: Pdb
references: 1dvj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dvj
catalytic residue: LYS 72

1dvjB
type: Pdb
references: 1dvj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dvj
catalytic residue: LYS 72

1dvjC
type: Pdb
references: 1dvj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dvj
catalytic residue: LYS 72

1dvjD
type: Pdb
references: 1dvj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dvj
catalytic residue: LYS 72

1eixA
type: Pdb
references: 1eix
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eix
catalytic residue: LYS 73

1eixB
type: Pdb
references: 1eix
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eix
catalytic residue: LYS 73

1eixC
type: Pdb
references: 1eix
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eix
catalytic residue: LYS 73

1eixD
type: Pdb
references: 1eix
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eix
catalytic residue: LYS 73

1jjkA
type: Pdb
references: 1jjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jjk
catalytic residue: LYS 73

1jjkB
type: Pdb
references: 1jjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jjk
catalytic residue: LYS 73

1jjkC
type: Pdb
references: 1jjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jjk
catalytic residue: LYS 73

1jjkD
type: Pdb
references: 1jjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jjk
catalytic residue: LYS 73

1jjkE
type: Pdb
references: 1jjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jjk
catalytic residue: LYS 73

1jjkF
type: Pdb
references: 1jjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jjk
catalytic residue: LYS 73

1jjkG
type: Pdb
references: 1jjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jjk
catalytic residue: LYS 73

1jjkH
type: Pdb
references: 1jjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jjk
catalytic residue: LYS 73

1jjkI
type: Pdb
references: 1jjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jjk
catalytic residue: LYS 73

1jjkJ
type: Pdb
references: 1jjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jjk
catalytic residue: LYS 73

1jjkK
type: Pdb
references: 1jjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jjk
catalytic residue: LYS 73

1jjkL
type: Pdb
references: 1jjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jjk
catalytic residue: LYS 73

1jjkM
type: Pdb
references: 1jjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jjk
catalytic residue: LYS 73

1jjkN
type: Pdb
references: 1jjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jjk
catalytic residue: LYS 73

1jjkO
type: Pdb
references: 1jjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jjk
catalytic residue: LYS 73

1jjkP
type: Pdb
references: 1jjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jjk
catalytic residue: LYS 73

1l2uA
type: Pdb
references: 1l2u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1l2u
catalytic residue: LYS 73

1l2uB
type: Pdb
references: 1l2u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1l2u
catalytic residue: LYS 73

Dependence of the catalytic activities on the aggregation and conformation states of uridine 5'-phosphate synthase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6894094
journal: Biochemistry
volume: 19
pages: 6068-74
published year: 1980
authors:
  item: Traut TW
  item: Payne RC

Dependence of the aggregation and conformation states of uridine 5'-phosphate synthase on pyrimidine nucleotides. Evidence for a regulatory site.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6894093
journal: Biochemistry
volume: 19
pages: 6062-8
published year: 1980
authors:
  item: Traut TW
  item: Payne RC
  item: Jones ME

Orotidine-5'-monophosphate decarboxylase catalysis: kinetic isotope effects and the state of hybridization of a bound transition-state analogue.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2334689
journal: Biochemistry
volume: 29
pages: 3198-202
published year: 1990
authors:
  item: Acheson SA
  item: Bell JB
  item: Jones ME
  item: Wolfenden R

Crystallization of yeast orotidine 5'-monophosphate decarboxylase complexed with 1-(5'-phospho-beta-D-ribofuranosyl) barbituric acid.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2008434
journal: Proteins
volume: 9
pages: 143-51
published year: 1991
authors:
  item: Bell JB
  item: Jones ME
  item: Carter CW Jr

Orotidylate decarboxylase: insights into the catalytic mechanism from substrate specificity studies.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1457411
journal: Biochemistry
volume: 31
pages: 12155-61
published year: 1992
authors:
  item: Shostak K
  item: Jones ME

A unique catalytic and inhibitor-binding role for Lys93 of yeast orotidylate decarboxylase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1457412
journal: Biochemistry
volume: 31
pages: 12162-8
published year: 1992
authors:
  item: Smiley JA
  item: Jones ME

Orotidylate decarboxylase of yeast and man.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1499340
journal: Curr Top Cell Regul
volume: 33
pages: 331-42
published year: 1992
authors:
  item: Jones ME

Intrinsic activity and stability of bifunctional human UMP synthase and its two separate catalytic domains, orotate phosphoribosyltransferase and orotidine-5'-phosphate decarboxylase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8631878
journal: J Biol Chem
volume: 271
pages: 10704-8
published year: 1996
authors:
  item: Yablonski MJ
  item: Pasek DA
  item: Han BD
  item: Jones ME
  item: Traut TW

A proficient enzyme revisited: the predicted mechanism for orotidine monophosphate decarboxylase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9139656
journal: Science
volume: 276
pages: 942-5
published year: 1997
authors:
  item: Lee JK
  item: Houk KN

No metal cofactor in orotidine 5'-monophosphate decarboxylase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10334928
journal: Biochem Biophys Res Commun
volume: 259
pages: 133-5
published year: 1999
authors:
  item: Cui W
  item: DeWitt JG
  item: Miller SM
  item: Wu W

Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5'-monophosphate decarboxylase.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10757968
journal: Biochemistry
volume: 39
pages: 4217-24
published year: 2000
authors:
  item: Harris P
  item: Navarro Poulsen JC
  item: Jensen KF
  item: Larsen S
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Contribution of enzyme-phosphoribosyl contacts to catalysis by orotidine 5'-phosphate decarboxylase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10889016
journal: Biochemistry
volume: 39
pages: 8113-8
published year: 2000
authors:
  item: Miller BG
  item: Snider MJ
  item: Short SA
  item: Wolfenden R

Yeast orotidine-5'-phosphate decarboxylase: steady-state and pre-steady-state analysis of the kinetic mechanism of substrate decarboxylation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10995247
journal: Biochemistry
volume: 39
pages: 11788-800
published year: 2000
authors:
  item: Porter DJ
  item: Short SA

Determination of the mechanism of orotidine 5'-monophosphate decarboxylase by isotope effects.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10769111
journal: Biochemistry
volume: 39
pages: 4569-74
published year: 2000
authors:
  item: Rishavy MA
  item: Cleland WW

Remarkable rate enhancement of orotidine 5'-monophosphate decarboxylase is due to transition-state stabilization rather than to ground-state destabilization.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11101287
journal: Biochemistry
volume: 39
pages: 14728-38
published year: 2000
authors:
  item: Warshel A
  item: Strajbl M
  item: Villa J
  item: Florian J

The structural basis for the remarkable catalytic proficiency of orotidine 5'-monophosphate decarboxylase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11114509
journal: Curr Opin Struct Biol
volume: 10
pages: 711-8
published year: 2000
authors:
  item: Begley TP
  item: Appleby TC
  item: Ealick SE

The crystal structure and mechanism of orotidine 5'-monophosphate decarboxylase.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10681442
journal: Proc Natl Acad Sci U S A
volume: 97
pages: 2005-10
published year: 2000
authors:
  item: Appleby TC
  item: Kinsland C
  item: Begley TP
  item: Ealick SE
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Anatomy of a proficient enzyme: the structure of orotidine 5'-monophosphate decarboxylase in the presence and absence of a potential transition state analog.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
medline id: 20160896
references: http://www.ncbi.nlm.nih.gov/pubmed/10681417
journal: Proc Natl Acad Sci U S A
volume: 97
pages: 2011-6
published year: 2000
authors:
  item: Miller BG
  item: Hassell AM
  item: Wolfenden R
  item: Milburn MV
  item: Short SA
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P03962

Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
medline id: 20160897
references: http://www.ncbi.nlm.nih.gov/pubmed/10681441
journal: Proc Natl Acad Sci U S A
volume: 97
pages: 2017-22
published year: 2000
authors:
  item: Wu N
  item: Mo Y
  item: Gao J
  item: Pai EF
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: O26232

Selenomethionine substitution of orotidine-5'-monophosphate decarboxylase causes a change in crystal contacts and space group.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11526316
journal: Acta Crystallogr D Biol Crystallogr
volume: 57
pages: 1251-9
published year: 2001
authors:
  item: Poulsen JC
  item: Harris P
  item: Jensen KF
  item: Larsen S
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Role of enzyme-ribofuranosyl contacts in the ground state and transition state for orotidine 5'-phosphate decarboxylase: a role for substrate destabilization?
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11371183
journal: Biochemistry
volume: 40
pages: 6227-32
published year: 2001
authors:
  item: Miller BG
  item: Butterfoss GL
  item: Short SA
  item: Wolfenden R

A reexamination of the substrate utilization of 2-thioorotidine-5'-monophosphate by yeast orotidine-5'-monophosphate decarboxylase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11300698
journal: Bioorg Chem
volume: 29
pages: 96-106
published year: 2001
authors:
  item: Smiley JA
  item: Hay KM
  item: Levison BS

Crystal structures of orotidine monophosphate decarboxylase: does the structure reveal the mechanism of nature's most proficient enzyme?
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11828434
journal: Chembiochem
volume: 2
pages: 113-8
published year: 2001
authors:
  item: Houk KN
  item: Lee JK
  item: Tantillo DJ
  item: Bahmanyar S
  item: Hietbrink BN

An alternative explanation for the catalytic proficiency of orotidine 5'-phosphate decarboxylase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11749542
journal: J Am Chem Soc
volume: 123
pages: 12837-48
published year: 2001
authors:
  item: Lee TS
  item: Chong LT
  item: Chodera JD
  item: Kollman PA

Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11278904
journal: J Biol Chem
volume: 276
pages: 15174-6
published year: 2001
authors:
  item: Miller BG
  item: Snider MJ
  item: Wolfenden R
  item: Short SA

Catalytic proficiency: the unusual case of OMP decarboxylase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12045113
journal: Annu Rev Biochem
volume: 71
pages: 847-85
published year: 2002
authors:
  item: Miller BG
  item: Wolfenden R

Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11900527
journal: Biochemistry
volume: 41
pages: 3861-9
published year: 2002
authors:
  item: Wise E
  item: Yew WS
  item: Babbitt PC
  item: Gerlt JA
  item: Rayment I

Mapping the active site-ligand interactions of orotidine 5'-monophosphate decarboxylase by crystallography.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11900543
journal: Biochemistry
volume: 41
pages: 4002-11
published year: 2002
authors:
  item: Wu N
  item: Gillon W
  item: Pai EF

The gas phase proton affinity of uracil: measuring multiple basic sites and implications for the enzyme mechanism of orotidine 5'-monophosphate decarboxylase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12430437
journal: Chem Commun (Camb)
volume: (20)
pages: 2354-5
published year: 2002
authors:
  item: Kurinovich MA
  item: Phillips LM
  item: Sharma S
  item: Lee JK

Crystal structures of inhibitor complexes reveal an alternate binding mode in orotidine-5'-monophosphate decarboxylase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12011084
journal: J Biol Chem
volume: 277
pages: 28080-7
published year: 2002
authors:
  item: Wu N
  item: Pai EF

Substrate binding induces domain movements in orotidine 5'-monophosphate decarboxylase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12054799
journal: J Mol Biol
volume: 318
pages: 1019-29
published year: 2002
authors:
  item: Harris P
  item: Poulsen JC
  item: Jensen KF
  item: Larsen S
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Hydrogen isotope tracing in the reaction of orotidine-5'-monophosphate decarboxylase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12667491
journal: Arch Biochem Biophys
volume: 412
pages: 267-71
published year: 2003
authors:
  item: Smiley JA
  item: DelFraino BJ
  item: Simpson BA

orotidine-5'-monophosphate decarboxylase
type: KeggEnzyme

orotodylate decarboxylase
type: KeggEnzyme

orotidine phosphate decarboxylase
type: KeggEnzyme

OMP decarboxylase
type: KeggEnzyme

orotate monophosphate decarboxylase
type: KeggEnzyme

orotidine monophosphate decarboxylase
type: KeggEnzyme

orotidine phosphate decarboxylase
type: KeggEnzyme

OMP-DC
type: KeggEnzyme

orotate decarboxylase
type: KeggEnzyme

orotidine 5'-phosphate decarboxylase
type: KeggEnzyme

orotidylic decarboxylase
type: KeggEnzyme

orotidylic acid decarboxylase
type: KeggEnzyme

orotodylate decarboxylase
type: KeggEnzyme

ODCase
type: KeggEnzyme

orotic decarboxylase
type: KeggEnzyme

orotidine-5'-phosphate carboxy-lyase
type: KeggEnzyme

Analogue
compound: Orotidine 5'-phosphate
pdb: 1eixA
ligand het code: BMQ

Analogue
compound: Orotidine 5'-phosphate
pdb: 1eixB
ligand het code: BMQ

Analogue
compound: Orotidine 5'-phosphate
pdb: 1eixC
ligand het code: BMQ

Analogue
compound: Orotidine 5'-phosphate
pdb: 1eixD
ligand het code: BMQ

Analogue
compound: UMP
pdb: 1dvjA
ligand het code: UP6

Analogue
compound: UMP
pdb: 1dvjB
ligand het code: UP6

Analogue
compound: UMP
pdb: 1dvjC
ligand het code: UP6

Analogue
compound: UMP
pdb: 1dvjD
ligand het code: UP6

TransitionStateAnalogue
pdb: 1dqxA
ligand het code: BMP

TransitionStateAnalogue
pdb: 1dqxB
ligand het code: BMP

TransitionStateAnalogue
pdb: 1dqxC
ligand het code: BMP

TransitionStateAnalogue
pdb: 1dqxD
ligand het code: BMP

TransitionStateAnalogue
pdb: 1jjkA
ligand het code: BMP

TransitionStateAnalogue
pdb: 1jjkB
ligand het code: BMP

TransitionStateAnalogue
pdb: 1jjkC
ligand het code: BMP

TransitionStateAnalogue
pdb: 1jjkD
ligand het code: BMP

TransitionStateAnalogue
pdb: 1jjkE
ligand het code: BMP

TransitionStateAnalogue
pdb: 1jjkF
ligand het code: BMP

TransitionStateAnalogue
pdb: 1jjkG
ligand het code: BMP

TransitionStateAnalogue
pdb: 1jjkH
ligand het code: BMP

TransitionStateAnalogue
pdb: 1jjkI
ligand het code: BMP

TransitionStateAnalogue
pdb: 1jjkJ
ligand het code: BMP

TransitionStateAnalogue
pdb: 1jjkK
ligand het code: BMP

TransitionStateAnalogue
pdb: 1jjkL
ligand het code: BMP

TransitionStateAnalogue
pdb: 1jjkM
ligand het code: BMP

TransitionStateAnalogue
pdb: 1jjkN
ligand het code: BMP

TransitionStateAnalogue
pdb: 1jjkO
ligand het code: BMP

TransitionStateAnalogue
pdb: 1jjkP
ligand het code: BMP

ReferenceForCatalyticMechanism
reference index: 6
reference section: p.12167-12168

ReferenceForCatalyticMechanism
reference index: 7
reference section: p.336-341

ReferenceForCatalyticMechanism
reference index: 9

ReferenceForCatalyticMechanism
reference index: 11
reference section: Fig.6, Fig.7, p.4222-4224
reference step: 2

ReferenceForCatalyticMechanism
reference index: 12
reference section: p.8116-8117

ReferenceForCatalyticMechanism
reference index: 14
reference section: Fig.3, Fig.4, Fig.5, p.4572-4574

ReferenceForCatalyticMechanism
reference index: 15
reference section: p.14731-14733

ReferenceForCatalyticMechanism
reference index: 16
reference section: Fig.2, p.714-716

ReferenceForCatalyticMechanism
reference index: 17
reference section: Scheme 1, Fig.7, p.2009-2010
reference step: 2

ReferenceForCatalyticMechanism
reference index: 18
reference section: Fig.7, p.2014-2016
reference step: 3

ReferenceForCatalyticMechanism
reference index: 19
reference section: Scheme II, p.2020-2022
reference step: 3

ReferenceForCatalyticMechanism
reference index: 20

ReferenceForCatalyticMechanism
reference index: 22
reference section: Fig.1, Fig.2, p.104-105

ReferenceForCatalyticMechanism
reference index: 23
reference section: Scheme 3, Scheme 4, p.114-118

ReferenceForCatalyticMechanism
reference index: 24
reference section: Fig.12, p.12846-12848

ReferenceForCatalyticMechanism
reference index: 26
reference section: Fig.8, p.863-874

ReferenceForCatalyticMechanism
reference index: 32
reference section: Fig. 1
reference step: p.268