M00225
type: Enzyme
cath: Urease, subunit C; domain 1
cath: TIM Barrel
cath: Urease, subunit B
cath: Urease; subunit A
ec: https://purl.uniprot.org/enzyme/3.5.1.5
uniprot: P69996
uniprot: D3UJ80
uniprot: P14916
uniprot: D3UJ81
kegg enzyme: Urease
kegg pathway: Urea cycle and metabolism of amino groups
kegg pathway: Purine metabolism
kegg pathway: Atrazine degradation
kegg cofactor: Nickel
kegg substrate: Urea
kegg substrate: H2O
kegg product: CO2
kegg product: NH3
kegg intermediate: Diaminohydroxymethanolate
kegg intermediate: Carbamate
pdb: 1e9yB01
pdb: 1e9zB01
pdb: 3qgaC01
pdb: 3qgaF01
pdb: 3qgaI01
pdb: 3qgaL01
pdb: 3qgaO01
pdb: 3qgaR01
pdb: 3qgkC01
pdb: 3qgkF01
pdb: 3qgkI01
pdb: 3qgkL01
pdb: 3qgkO01
pdb: 3qgkR01
pdb: 1e9yB02
pdb: 1e9zB02
pdb: 3qgaC02
pdb: 3qgaF02
pdb: 3qgaI02
pdb: 3qgaL02
pdb: 3qgaO02
pdb: 3qgaR02
pdb: 3qgkC02
pdb: 3qgkF02
pdb: 3qgkI02
pdb: 3qgkL02
pdb: 3qgkO02
pdb: 3qgkR02
pdb: 1e9yA01
pdb: 1e9zA01
pdb: 3qgaA02
pdb: 3qgaD02
pdb: 3qgaG02
pdb: 3qgaJ02
pdb: 3qgaM02
pdb: 3qgaP02
pdb: 3qgkA02
pdb: 3qgkD02
pdb: 3qgkG02
pdb: 3qgkJ02
pdb: 3qgkM02
pdb: 3qgkP02
pdb: 1e9yA02
pdb: 1e9zA02
pdb: 3qgaA01
pdb: 3qgaD01
pdb: 3qgaG01
pdb: 3qgaJ01
pdb: 3qgaM01
pdb: 3qgaP01
pdb: 3qgkA01
pdb: 3qgkD01
pdb: 3qgkG01
pdb: 3qgkJ01
pdb: 3qgkM01
pdb: 3qgkP01
active site residues resources: Plant ureases: roles and regulation.
active site residues resources: Interaction of Urea with a Hydroxide-Bridged Dinuclear Nickel Center:? An Alternative Model for the Mechanism of Urease.
active site residues resources: Interallelic complementation at the ubiquitous urease coding locus of soybean.

Urease, subunit C; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.30.40.10

TIM Barrel
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.20.20.140
catalytic domain: index.html

Urease, subunit B
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.10.150.10

Urease; subunit A
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.280.10

Urea cycle and metabolism of amino groups
type: KeggPathway
references: KEGG:MAP00220

Purine metabolism
type: KeggPathway
references: KEGG:MAP00230

Atrazine degradation
type: KeggPathway
references: KEGG:MAP00791

Nickel
type: KeggCofactor
references: KEGG:C00291
references: CHEBI:28112
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: heavy metal

Urea
type: KeggSubstrate
references: KEGG:C00086
references: CHEBI:16199
references: CHEBI:48376
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: amide group
compound type: amine group

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

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

NH3
type: KeggProduct
references: KEGG:C00014
references: CHEBI:16134
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: amine group
compound type: organic ion

Diaminohydroxymethanolate
type: KeggIntermediate
references: KEGG:I00127

Carbamate
type: KeggIntermediate
references: KEGG:C01563

1e9yB02
type: Pdb
references: 1e9y
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e9y
catalytic residue: HIS 221;ASP 223;HIS 322;ARG 338
cofactor binding residue: KCX 219(Nickel-1 & -2);HIS 248;HIS 274(Nickel-1);HIS 136;HIS 138;ASP 362(Nickel-2)
modified residue: KCX 219(Carbamylated LYS)

1e9zB02
type: Pdb
references: 1e9z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e9z
catalytic residue: HIS 221;ASP 223;HIS 322;ARG 338
cofactor binding residue: KCX 219(Nickel-1 & -2);HIS 248;HIS 274(Nickel-1);HIS 136;HIS 138;ASP 362(Nickel-2)
modified residue: KCX 219(Carbamylated LYS)

3qgaC02
type: Pdb
references: 3qga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qga
catalytic residue: HIS 220;ASP 222;HIS 321;ARG 337
cofactor binding residue: KCX 218(Nickel-1 & -2);HIS 247;HIS 273(Nickel-1);HIS 135;HIS 137;ASP 361(Nickel-2)
modified residue: KCX 218(Carbamylated LYS)
comment: invisible 329-332

3qgaF02
type: Pdb
references: 3qga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qga
catalytic residue: HIS 220;ASP 222;HIS 321;ARG 337
cofactor binding residue: KCX 218(Nickel-1 & -2);HIS 247;HIS 273(Nickel-1);HIS 135;HIS 137;ASP 361(Nickel-2)
modified residue: KCX 218(Carbamylated LYS)
comment: invisible 329-332

3qgaI02
type: Pdb
references: 3qga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qga
catalytic residue: HIS 220;ASP 222;HIS 321;ARG 337
cofactor binding residue: KCX 218(Nickel-1 & -2);HIS 247;HIS 273(Nickel-1);HIS 135;HIS 137;ASP 361(Nickel-2)
modified residue: KCX 218(Carbamylated LYS)
comment: invisible 329-332

3qgaL02
type: Pdb
references: 3qga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qga
catalytic residue: HIS 220;ASP 222;HIS 321;ARG 337
cofactor binding residue: KCX 218(Nickel-1 & -2);HIS 247;HIS 273(Nickel-1);HIS 135;HIS 137;ASP 361(Nickel-2)
modified residue: KCX 218(Carbamylated LYS)
comment: invisible 329-332

3qgaO02
type: Pdb
references: 3qga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qga
catalytic residue: HIS 220;ASP 222;HIS 321;ARG 337
cofactor binding residue: KCX 218(Nickel-1 & -2);HIS 247;HIS 273(Nickel-1);HIS 135;HIS 137;ASP 361(Nickel-2)
modified residue: KCX 218(Carbamylated LYS)
comment: invisible 329-332

3qgaR02
type: Pdb
references: 3qga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qga
catalytic residue: HIS 220;ASP 222;HIS 321;ARG 337
cofactor binding residue: KCX 218(Nickel-1 & -2);HIS 247;HIS 273(Nickel-1);HIS 135;HIS 137;ASP 361(Nickel-2)
modified residue: KCX 218(Carbamylated LYS)
comment: invisible 329-332

3qgkC02
type: Pdb
references: 3qgk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qgk
catalytic residue: HIS 220;ASP 222;HIS 321;ARG 337
cofactor binding residue: KCX 218(Nickel-1 & -2);HIS 247;HIS 273(Nickel-1);HIS 135;HIS 137;ASP 361(Nickel-2)
modified residue: KCX 218(Carbamylated LYS)
comment: invisible 329-332

3qgkF02
type: Pdb
references: 3qgk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qgk
catalytic residue: HIS 220;ASP 222;HIS 321;ARG 337
cofactor binding residue: KCX 218(Nickel-1 & -2);HIS 247;HIS 273(Nickel-1);HIS 135;HIS 137;ASP 361(Nickel-2)
modified residue: KCX 218(Carbamylated LYS)
comment: invisible 329-332

3qgkI02
type: Pdb
references: 3qgk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qgk
catalytic residue: HIS 220;ASP 222;HIS 321;ARG 337
cofactor binding residue: KCX 218(Nickel-1 & -2);HIS 247;HIS 273(Nickel-1);HIS 135;HIS 137;ASP 361(Nickel-2)
modified residue: KCX 218(Carbamylated LYS)
comment: invisible 329-332

3qgkL02
type: Pdb
references: 3qgk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qgk
catalytic residue: HIS 220;ASP 222;HIS 321;ARG 337
cofactor binding residue: KCX 218(Nickel-1 & -2);HIS 247;HIS 273(Nickel-1);HIS 135;HIS 137;ASP 361(Nickel-2)
modified residue: KCX 218(Carbamylated LYS)
comment: invisible 329-332

3qgkO02
type: Pdb
references: 3qgk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qgk
catalytic residue: HIS 220;ASP 222;HIS 321;ARG 337
cofactor binding residue: KCX 218(Nickel-1 & -2);HIS 247;HIS 273(Nickel-1);HIS 135;HIS 137;ASP 361(Nickel-2)
modified residue: KCX 218(Carbamylated LYS)
comment: invisible 329-332

3qgkR02
type: Pdb
references: 3qgk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qgk
catalytic residue: HIS 220;ASP 222;HIS 321;ARG 337
cofactor binding residue: KCX 218(Nickel-1 & -2);HIS 247;HIS 273(Nickel-1);HIS 135;HIS 137;ASP 361(Nickel-2)
modified residue: KCX 218(Carbamylated LYS)
comment: invisible 329-332

Plant ureases: roles and regulation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11996109
journal: Acta Biochim Pol
volume: 47
pages: 1189-95
published year: 2000
authors:
  item: Sirko A
  item: Brodzik R

Interaction of Urea with a Hydroxide-Bridged Dinuclear Nickel Center:? An Alternative Model for the Mechanism of Urease.
type: BibliographicResource
journal: J Am Chem Soc
volume: 122
pages: 9172-77
published year: 2000
authors:
  item: Barrios AM
  item: Lippard SJ

Interallelic complementation at the ubiquitous urease coding locus of soybean.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12913138
journal: Plant Physiol
volume: 132
pages: 1801-10
published year: 2003
authors:
  item: Goldraij A
  item: Beamer LJ
  item: Polacco JC

ReferenceForCatalyticMechanism
reference index: 7
reference section: figure, p.996

ReferenceForCatalyticMechanism
reference index: 12
reference section: Figure 2, Figure 6, p.333-337

ReferenceForCatalyticMechanism
reference index: 17
reference section: Figure 8, p.211-213

ReferenceForCatalyticMechanism
reference index: 19
reference section: Figure 7, p.5394-5395

ReferenceForCatalyticMechanism
reference index: 20
reference section: FIGURE 1, FIGURE 8, p.8583-8584

ReferenceForCatalyticMechanism
reference index: 22
reference section: Figure 2, Figure 3, Figure 4, p.796

ReferenceForCatalyticMechanism
reference index: 23

ReferenceForCatalyticMechanism
reference index: 24
reference section: Fig.6, p.787

ReferenceForCatalyticMechanism
reference index: 31
reference section: Figure 3, Figure 7, Figure 8, Figure 10, p.15335-15337

ReferenceForCatalyticMechanism
reference index: 34
reference section: Figure 13, p.6943

ReferenceForCatalyticMechanism
reference index: 35
reference section: Figure 4, Figure 11, p.11842

ReferenceForCatalyticMechanism
reference index: 36
reference section: Figure 4, Figure 5, Figure 6, Figure 13, Figure 16, Figure 18

ReferenceForCatalyticMechanism
reference index: 37
reference section: Figure 1, Figure 2, Figure 3

ReferenceForCatalyticMechanism
reference index: 40
reference section: Scheme 2, p.521

Site-directed mutagenesis of the active site cysteine in Klebsiella aerogenes urease.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1400317
journal: J Biol Chem
volume: 267
pages: 20024-7
published year: 1992
authors:
  item: Martin PR
  item: Hausinger RP

Preliminary crystallographic studies of urease from jack bean and from Klebsiella aerogenes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1404395
journal: J Mol Biol
volume: 227
pages: 934-7
published year: 1992
authors:
  item: Jabri E
  item: Lee MH
  item: Hausinger RP
  item: Karplus PA

Site-directed mutagenesis of Klebsiella aerogenes urease: identification of histidine residues that appear to function in nickel ligation, substrate binding, and catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8318888
journal: Protein Sci
volume: 2
pages: 1034-41
published year: 1993
authors:
  item: Park IS
  item: Hausinger RP

Molecular biology of microbial ureases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7565414
journal: Microbiol Rev
volume: 59
pages: 451-80
published year: 1995
authors:
  item: Mobley HL
  item: Island MD
  item: Hausinger RP

Urease activity in the crystalline state.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8535259
journal: Protein Sci
volume: 4
pages: 2234-6
published year: 1995
authors:
  item: Moncrief MB
  item: Hom LG
  item: Jabri E
  item: Karplus PA
  item: Hausinger RP

The crystal structure of urease from Klebsiella aerogenes.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
medline id: 95273988
references: http://www.ncbi.nlm.nih.gov/pubmed/7754395
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P18314
references: P18315
references: P18316
journal: Science
volume: 268
pages: 998-1004
published year: 1995
authors:
  item: Jabri E
  item: Carr MB
  item: Hausinger RP
  item: Karplus PA

At last--the crystal structure of urease.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7754394
journal: Science
volume: 268
pages: 996-7
published year: 1995
authors:
  item: Lippard SJ

Structures of the Klebsiella aerogenes urease apoenzyme and two active-site mutants.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
medline id: 96346054
references: http://www.ncbi.nlm.nih.gov/pubmed/8718850
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P18314
references: P18315
references: P18316
journal: Biochemistry
volume: 35
pages: 10616-26
published year: 1996
authors:
  item: Jabri E
  item: Karplus PA

Characterization of the mononickel metallocenter in H134A mutant urease.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/8702515
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Biol Chem
volume: 271
pages: 18632-7
published year: 1996
authors:
  item: Park IS
  item: Michel LO
  item: Pearson MA
  item: Jabri E
  item: Karplus PA
  item: Wang S
  item: Dong J
  item: Scott RA
  item: Koehler BP
  item: Johnson MK
  item: Hausinger RP

Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/9201965
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biochemistry
volume: 36
pages: 8164-72
published year: 1997
authors:
  item: Pearson MA
  item: Michel LO
  item: Hausinger RP
  item: Karplus PA

An evolutionary treasure: unification of a broad set of amidohydrolases related to urease.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9144792
journal: Proteins
volume: 28
pages: 72-82
published year: 1997
authors:
  item: Holm L
  item: Sander C

70 Years of Crystalline Urease:? What Have We Learned?
type: BibliographicResource
journal: Acc Chem Res
volume: 30
pages: 330?7
published year: 1997
authors:
  item: Karplus PA
  item: Pearson MA
  item: Hausinger RP

Crystallization and preliminary high-resolution X-ray diffraction analysis of native and beta-mercaptoethanol-inhibited urease from Bacillus pasteurii.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
references: http://www.ncbi.nlm.nih.gov/pubmed/9761912
references: P41020
references: P41021
references: P41022
journal: Acta Crystallogr D Biol Crystallogr
volume: 54
pages: 409-12
published year: 1998
authors:
  item: Benini S
  item: Ciurli S
  item: Rypniewski WR
  item: Wilson KS
  item: Mangani S

Chemical rescue of Klebsiella aerogenes urease variants lacking the carbamylated-lysine nickel ligand.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
medline id: 98226663
references: http://www.ncbi.nlm.nih.gov/pubmed/9558361
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P18314
references: P18315
references: P18316
journal: Biochemistry
volume: 37
pages: 6214-20
published year: 1998
authors:
  item: Pearson MA
  item: Schaller RA
  item: Michel LO
  item: Karplus PA
  item: Hausinger RP

The complex of Bacillus pasteurii urease with beta-mercaptoethanol from X-ray data at 1.65-angstrom resolution.
type: BibliographicResource
comment: X-ray crystallography
journal: J Biol Inorg Chem
volume: 3
pages: 268-73
published year: 1998
authors:
  item: Benini S
  item: Rypniewski WR
  item: Wilson KS
  item: Ciurli S
  item: Mangani S
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Characterization of metal-substituted Klebsiella aerogenes urease.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
references: http://www.ncbi.nlm.nih.gov/pubmed/10555581
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P18314
references: P18315
references: P18316
journal: J Biol Inorg Chem
volume: 4
pages: 468-77
published year: 1999
authors:
  item: Yamaguchi K
  item: Cosper NJ
  item: Stalhandske C
  item: Scott RA
  item: Pearson MA
  item: Karplus PA
  item: Hausinger RP

A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
medline id: 99148127
references: http://www.ncbi.nlm.nih.gov/pubmed/10368287
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P41020
references: P41021
references: P41022
journal: Structure Fold Des
volume: 7
pages: 205-16
published year: 1999
authors:
  item: Benini S
  item: Rypniewski WR
  item: Wilson KS
  item: Miletti S
  item: Ciurli S
  item: Mangani S

Fluoride inhibition of Klebsiella aerogenes urease: mechanistic implications of a pseudo-uncompetitive, slow-binding inhibitor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10820010
journal: Biochemistry
volume: 39
pages: 5389-96
published year: 2000
authors:
  item: Todd MJ
  item: Hausinger RP

Kinetic and structural characterization of urease active site variants.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND MUTAGENESIS OF HIS-219; ASP-221; HIS-320 AND ARG-336.
references: http://www.ncbi.nlm.nih.gov/pubmed/10913264
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P18314
references: P18315
references: P18316
journal: Biochemistry
volume: 39
pages: 8575-84
published year: 2000
authors:
  item: Pearson MA
  item: Park IS
  item: Schaller RA
  item: Michel LO
  item: Karplus PA
  item: Hausinger RP

The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 A resolution.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10766443
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Biol Inorg Chem
volume: 5
pages: 110-8
published year: 2000
authors:
  item: Benini S
  item: Rypniewski WR
  item: Wilson KS
  item: Miletti S
  item: Ciurli S
  item: Mangani S

Molecular mechanics evaluation of the proposed mechanisms for the degradation of urea by urease.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10798524
journal: J Biomol Struct Dyn
volume: 17
pages: 787-97
published year: 2000
authors:
  item: Zimmer M

Structure-based rationalization of urease inhibition by phosphate: novel insights into the enzyme mechanism.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11713685
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Biol Inorg Chem
volume: 6
pages: 778-90
published year: 2001
authors:
  item: Benini S
  item: Rypniewski WR
  item: Wilson KS
  item: Ciurli S
  item: Mangani S

Structure-based computational study of the catalytic and inhibition mechanisms of urease.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11315566
journal: J Biol Inorg Chem
volume: 6
pages: 300-14
published year: 2001
authors:
  item: Musiani F
  item: Arnofi E
  item: Casadio R
  item: Ciurli S

Helicobacter pylori springs another surprise.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11373609
journal: Nat Struct Biol
volume: 8
pages: 480-2
published year: 2001
authors:
  item: Dunn BE
  item: Grutter MG

Supramolecular assembly and acid resistance of Helicobacter pylori urease.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND SUBUNIT STRUCTURE.
references: http://www.ncbi.nlm.nih.gov/pubmed/11373617
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references: P14916
references: P69996
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pages: 505-9
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Decomposition of alkyl-substituted urea molecules at a hydroxide-bridged dinickel center.
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Crystallization and preliminary X-ray structure determination of jack bean urease with a bound antibody fragment.
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Three-dimensional quantitative structure-activity relationship and comparative molecular field analysis of dipeptide hydroxamic acid Helicobacter pylori urease inhibitors.
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Ureases: quantum chemical calculations on cluster models.
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Molecular details of urease inhibition by boric acid: insights into the catalytic mechanism.
type: BibliographicResource
comment: X-ray crystallography
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The hydrolysis of urea and the proficiency of urease.
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Enzymatic catalysis of urea decomposition: elimination or hydrolysis?
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Catalyzed decomposition of urea. Molecular dynamics simulations of the binding of urea to urease.
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Crystal structure of the first plant urease from jack bean: 83 years of journey from its first crystal to molecular structure.
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Iron-containing urease in a pathogenic bacterium.
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Chemistry of Ni2+ in urease: sensing, trafficking, and catalysis.
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pages: 520-30
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Urea amidohydrolase
type: KeggEnzyme

Analogue
compound: Nickel
pdb: 3qgaC02
ligand het code: 2x_FE

Analogue
compound: Nickel
pdb: 3qgaF02
ligand het code: 2x_FE

Analogue
compound: Nickel
pdb: 3qgaI02
ligand het code: 2x_FE

Analogue
compound: Nickel
pdb: 3qgaL02
ligand het code: 2x_FE

Analogue
compound: Nickel
pdb: 3qgaO02
ligand het code: 2x_FE

Analogue
compound: Nickel
pdb: 3qgaR02
ligand het code: 2x_FE

Analogue
compound: Nickel
pdb: 3qgkC02
ligand het code: 2x_FE

Analogue
compound: Nickel
pdb: 3qgkF02
ligand het code: 2x_FE

Analogue
compound: Nickel
pdb: 3qgkI02
ligand het code: 2x_FE

Analogue
compound: Nickel
pdb: 3qgkL02
ligand het code: 2x_FE

Analogue
compound: Nickel
pdb: 3qgkO02
ligand het code: 2x_FE

Analogue
compound: Nickel
pdb: 3qgkR02
ligand het code: 2x_FE

IntermediateAnalogue
compound: Carbamate
pdb: 1e9yB02
ligand het code: HAE