S00539
type: Enzyme
rlcp: p111
rlcp: p120
cath: TIM Barrel
ec: https://purl.uniprot.org/enzyme/4.2.1.24
uniprot: Q59334
kegg enzyme: porphobilinogen synthase
kegg enzyme: aminolevulinate dehydratase
kegg enzyme: delta-aminolevulinate dehydratase
kegg enzyme: delta-aminolevulinic acid dehydrase
kegg enzyme: delta-aminolevulinic acid dehydratase
kegg enzyme: aminolevulinic dehydratase
kegg enzyme: delta-aminolevulinic dehydratase
kegg enzyme: 5-levulinic acid dehydratase
kegg enzyme: 5-aminolevulinate hydro-lyase (adding 5-aminolevulinate andcyclizing)
kegg pathway: Porphyrin and chlorophyll metabolism
kegg cofactor: Magnesium
kegg substrate: 5-Aminolevulinate
kegg product: Porphobilinogen
kegg product: H2O
pdb: 1w1zA
pdb: 1w1zB
pdb: 2c1hA
pdb: 2c1hB
pdb bound state: Unbound
  compound: 5-Aminolevulinate
  pdb: 1w1zA
pdb bound state: Unbound
  compound: 5-Aminolevulinate
  pdb: 1w1zB
pdb bound state: Unbound
  compound: 5-Aminolevulinate
  pdb: 2c1hA
pdb bound state: Unbound
  compound: 5-Aminolevulinate
  pdb: 2c1hB
pdb bound state: Unbound
  compound: Porphobilinogen
  pdb: 1w1zA
pdb bound state: Unbound
  compound: Porphobilinogen
  pdb: 1w1zB
pdb bound state: Unbound
  compound: Porphobilinogen
  pdb: 2c1hA
pdb bound state: Unbound
  compound: Porphobilinogen
  pdb: 2c1hB
pdb bound state: Unbound
  pdb: 1w1zA
pdb bound state: Unbound
  pdb: 1w1zB
pdb bound state: Unbound
  pdb: 2c1hA
pdb bound state: Unbound
  pdb: 2c1hB
pdb bound state: IntermediateAnalogue
  pdb: 1w1zA
  ligand het code: LEA
references: 13C NMR as a probe for the study of enzyme-catalysed reactions: mechanism of action of 5-aminolevulinic acid dehydratase.
references: 13C NMR studies of porphobilinogen synthase: observation of intermediates bound to a 280,000-dalton protein.
references: 13C NMR studies of methylene and methine carbons of substrate bound to a 280,000-dalton protein, porphobilinogen synthase.
references: Small angle X-ray scattering study on bovine porphobilinogen synthase (5-aminolaevulinate dehydratase).
references: 15N and 13C NMR studies of ligands bound to the 280,000-dalton protein porphobilinogen synthase elucidate the structures of enzyme-bound product and a Schiff base intermediate.
references: Probing of active site residues of the zinc enzyme 5-aminolevulinate dehydratase by spin and fluorescence labels.
references: 5-Chlorolevulinate modification of porphobilinogen synthase identifies a potential role for the catalytic zinc.
references: Porphobilinogen synthase from Escherichia coli is a Zn(II) metalloenzyme stimulated by Mg(II).
references: Purification and characterization of 5-aminolaevulinic acid dehydratase from Escherichia coli and a study of the reactive thiols at the metal-binding domain.
references: Spatial proximity and sequence localization of the reactive sulfhydryls of porphobilinogen synthase.
references: 5-Chloro[1,4-13C]levulinic acid modification of mammalian and bacterial porphobilinogen synthase suggests an active site containing two Zn(II).
references: Characterization of the role of the stimulatory magnesium of Escherichia coli porphobilinogen synthase.
references: Porphobilinogen synthase, the first source of heme's asymmetry.
references: The phylogenetically conserved histidines of Escherichia coli porphobilinogen synthase are not required for catalysis.
references: Purification, metal cofactor, N-terminal sequence and subunit composition of a 5-aminolevulinic acid dehydratase from the unicellular green alga Scenedesmus obliquus, mutant C-2A'.
references: Magnetic resonance studies on the active site and metal centers of Bradyrhizobium japonicum porphobilinogen synthase.
references: X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase.
references: Crystallization of 5-aminolaevulinic acid dehydratase from Escherichia coli and Saccharomyces cerevisiae and preliminary X-ray characterization of the crystals.
references: Mechanistic studies on E.coli 5-aminolaevulinic acid dehydratase.
references: X-ray structure of 5-aminolevulinic acid dehydratase from Escherichia coli complexed with the inhibitor levulinic acid at 2.0 A resolution.
references: Production, purification, and characterization of a Mg2+-responsive porphobilinogen synthase from Pseudomonas aeruginosa.
references: Pseudomonas aeruginosa contains a novel type V porphobilinogen synthase with no required catalytic metal ions.
references: High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase.
references: The Schiff base complex of yeast 5-aminolaevulinic acid dehydratase with laevulinic acid.
references: MAD analyses of yeast 5-aminolaevulinate dehydratase: their use in structure determination and in defining the metal-binding sites.
references: Porphobilinogen synthase from pea: expression from an artificial gene, kinetic characterization, and novel implications for subunit interactions.
references: Inhibition of Escherichia coli porphobilinogen synthase using analogs of postulated intermediates.
references: Mechanistic basis for suicide inactivation of porphobilinogen synthase by 4,7-dioxosebacic acid, an inhibitor that shows dramatic species selectivity.
references: The X-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with two diacid inhibitors.
references: Mechanistic implications of mutations to the active site lysine of porphobilinogen synthase.
references: The x-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with substrate and three inhibitors.
references: Selenoxides inhibit delta-aminolevulinic acid dehydratase.
references: 5-Aminolaevulinic acid dehydratase: metals, mutants and mechanism.
references: Species-specific inhibition of porphobilinogen synthase by 4-oxosebacic acid.
references: Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism.
references: X-ray structure of a putative reaction intermediate of 5-aminolaevulinic acid dehydratase.
references: Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase.
references: The X-ray structure of the plant like 5-aminolaevulinic acid dehydratase from Chlorobium vibrioforme complexed with the inhibitor laevulinic acid at 2.6 A resolution.
references: Tracking the evolution of porphobilinogen synthase metal dependence in vitro.
references: Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid.
references: Structure of Chlorobium vibrioforme 5-aminolaevulinic acid dehydratase complexed with a diacid inhibitor.
references: Probing the active site of Pseudomonas aeruginosa porphobilinogen synthase using newly developed inhibitors.
comment: There are several subfamilies of the homologous enzymes, such as zinc-dependent (S00239, S00538 in EzCatDB), and zinc-independent (S00537, S00539) subfamilies. This enzyme belongs to zinc-independent subfamily. Although this enzyme binds magnesium ion, it is not directly involved in catalysis. According to the literature [35] and [42], the reaction proceeds as follows: (A) Exchange of double-bonded atoms; Schiff-base formation between Lys253 and P-side ALA substrate: (B) Exchange of double-bonded atoms; Schiff-base formation between Lys200 and A-side ALA substrate: (C) Isomerization; Shift of double-bond from N=C-C to N-C=C, forming an enamine intermediate at A-side: (D) Addition (C-C bond formation): (E) Exchange of double-bonded atoms; Exchange of Schiff-base (C-N bond formation & releasing Lys200): (F) Eliminative double-bond formation (releasing Lys253): (G) Isomerization; Shift of double-bonds from N=C-C=C-C to N-C=C-C=C: However, although the first three reactions (A-C) seem to be common to all the homologous enzymes (S00239, S00538, S00537 in EzCatDB), the rest of the reactions (D-G) have not been elucidated yet.

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

Porphyrin and chlorophyll metabolism
type: KeggPathway
references: KEGG:MAP00860

Magnesium
type: KeggCofactor
references: KEGG:C00305
compound type: divalent metal (Ca2+, Mg2+)
references: CHEBI:18420
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

5-Aminolevulinate
type: KeggSubstrate
references: KEGG:C00430
compound type: amino acids
compound type: carbohydrate
references: CHEBI:17549
references: CHEBI:356416
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Porphobilinogen
type: KeggProduct
references: KEGG:C00931
compound type: amine group
compound type: aromatic ring (with nitrogen atoms)
compound type: carboxyl group
references: CHEBI:17381
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

1w1zA
type: Pdb
references: 1w1z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1w1z
catalytic residue: ASP 123;SER 170;LYS 200;LYS 253
cofactor binding residue: GLU 238(Magnesium binding)

1w1zB
type: Pdb
references: 1w1z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1w1z
catalytic residue: ASP 123;SER 170;LYS 200;LYS 253
cofactor binding residue: GLU 238(Magnesium binding)

2c1hA
type: Pdb
references: 2c1h
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2c1h
catalytic residue: ASP 123;SER 170;LYS 200;LYS 253
cofactor binding residue: GLU 238(Magnesium binding)

2c1hB
type: Pdb
references: 2c1h
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2c1h
catalytic residue: ASP 123;SER 170;LYS 200;LYS 253
cofactor binding residue: GLU 238(Magnesium binding)

13C NMR as a probe for the study of enzyme-catalysed reactions: mechanism of action of 5-aminolevulinic acid dehydratase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6967019
journal: FEBS Lett
volume: 114
pages: 283-6
published year: 1980
authors:
  item: Jordan PM
  item: Seehra JS

13C NMR studies of porphobilinogen synthase: observation of intermediates bound to a 280,000-dalton protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3663587
journal: Biochemistry
volume: 26
pages: 4258-64
published year: 1987
authors:
  item: Jaffe EK
  item: Markham GD

13C NMR studies of methylene and methine carbons of substrate bound to a 280,000-dalton protein, porphobilinogen synthase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3166990
journal: Biochemistry
volume: 27
pages: 4475-81
published year: 1988
authors:
  item: Jaffe EK
  item: Markham GD

Small angle X-ray scattering study on bovine porphobilinogen synthase (5-aminolaevulinate dehydratase).
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3242540
journal: Biol Chem Hoppe Seyler
volume: 369
pages: 1099-103
published year: 1988
authors:
  item: Pilz I
  item: Schwarz E
  item: Vuga M
  item: Beyersmann D

15N and 13C NMR studies of ligands bound to the 280,000-dalton protein porphobilinogen synthase elucidate the structures of enzyme-bound product and a Schiff base intermediate.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2252894
journal: Biochemistry
volume: 29
pages: 8345-50
published year: 1990
authors:
  item: Jaffe EK
  item: Markham GD
  item: Rajagopalan JS

Probing of active site residues of the zinc enzyme 5-aminolevulinate dehydratase by spin and fluorescence labels.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1965291
journal: Biol Chem Hoppe Seyler
volume: 371
pages: 1145-52
published year: 1990
authors:
  item: Block C
  item: Lohmann RD
  item: Beyersmann D

5-Chlorolevulinate modification of porphobilinogen synthase identifies a potential role for the catalytic zinc.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1346974
journal: Biochemistry
volume: 31
pages: 2113-23
published year: 1992
authors:
  item: Jaffe EK
  item: Abrams WR
  item: Kaempfen HX
  item: Harris KA Jr

Porphobilinogen synthase from Escherichia coli is a Zn(II) metalloenzyme stimulated by Mg(II).
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8424649
journal: Arch Biochem Biophys
volume: 300
pages: 169-77
published year: 1993
authors:
  item: Mitchell LW
  item: Jaffe EK

Purification and characterization of 5-aminolaevulinic acid dehydratase from Escherichia coli and a study of the reactive thiols at the metal-binding domain.
type: BibliographicResource
comment: CHARACTERIZATION, AND SEQUENCE OF 1-5; 95-134 AND 237-253.
medline id: 93176130
references: http://www.ncbi.nlm.nih.gov/pubmed/8439296
journal: Biochem J
volume: 290
pages: 279-87
published year: 1993
authors:
  item: Spencer P
  item: Jordan PM
references: P15002

Spatial proximity and sequence localization of the reactive sulfhydryls of porphobilinogen synthase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8382991
journal: Protein Sci
volume: 2
pages: 71-9
published year: 1993
authors:
  item: Markham GD
  item: Myers CB
  item: Harris KA Jr
  item: Volin M
  item: Jaffe EK

5-Chloro[1,4-13C]levulinic acid modification of mammalian and bacterial porphobilinogen synthase suggests an active site containing two Zn(II).
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7918369
journal: Biochemistry
volume: 33
pages: 11554-62
published year: 1994
authors:
  item: Jaffe EK
  item: Volin M
  item: Myers CB
  item: Abrams WR

Characterization of the role of the stimulatory magnesium of Escherichia coli porphobilinogen synthase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7819203
journal: Biochemistry
volume: 34
pages: 244-51
published year: 1995
authors:
  item: Jaffe EK
  item: Ali S
  item: Mitchell LW
  item: Taylor KM
  item: Volin M
  item: Markham GD

Porphobilinogen synthase, the first source of heme's asymmetry.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7592564
journal: J Bioenerg Biomembr
volume: 27
pages: 169-79
published year: 1995
authors:
  item: Jaffe EK

The phylogenetically conserved histidines of Escherichia coli porphobilinogen synthase are not required for catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7592604
journal: J Biol Chem
volume: 270
pages: 24054-9
published year: 1995
authors:
  item: Mitchell LW
  item: Volin M
  item: Jaffe EK

Purification, metal cofactor, N-terminal sequence and subunit composition of a 5-aminolevulinic acid dehydratase from the unicellular green alga Scenedesmus obliquus, mutant C-2A'.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8612634
journal: Eur J Biochem
volume: 236
pages: 600-8
published year: 1996
authors:
  item: Stolz M
  item: Dornemann D

Magnetic resonance studies on the active site and metal centers of Bradyrhizobium japonicum porphobilinogen synthase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9341235
journal: Biochemistry
volume: 36
pages: 13421-7
published year: 1997
authors:
  item: Petrovich RM
  item: Jaffe EK

X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
medline id: 98069651
references: http://www.ncbi.nlm.nih.gov/pubmed/9406553
journal: Nat Struct Biol
volume: 4
pages: 1025-31
published year: 1997
authors:
  item: Erskine PT
  item: Senior N
  item: Awan S
  item: Lambert R
  item: Lewis G
  item: Tickle IJ
  item: Sarwar M
  item: Spencer P
  item: Thomas P
  item: Warren MJ
  item: Shoolingin-Jordan PM
  item: Wood SP
  item: Cooper JB
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P05373

Crystallization of 5-aminolaevulinic acid dehydratase from Escherichia coli and Saccharomyces cerevisiae and preliminary X-ray characterization of the crystals.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9260292
journal: Protein Sci
volume: 6
pages: 1774-6
published year: 1997
authors:
  item: Erskine PT
  item: Senior N
  item: Maignan S
  item: Cooper J
  item: Lambert R
  item: Lewis G
  item: Spencer P
  item: Awan S
  item: Warren M
  item: Tickle IJ
  item: Thomas P
  item: Wood SP
  item: Shoolingin-Jordan PM

Mechanistic studies on E.coli 5-aminolaevulinic acid dehydratase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9766004
journal: Biochem Soc Trans
volume: 26
pages: S285
published year: 1998
authors:
  item: Norton E
  item: Sarwar M
  item: Shoolingin-Jordan P

X-ray structure of 5-aminolevulinic acid dehydratase from Escherichia coli complexed with the inhibitor levulinic acid at 2.0 A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
medline id: 99211872
references: http://www.ncbi.nlm.nih.gov/pubmed/10194344
journal: Biochemistry
volume: 38
pages: 4266-76
published year: 1999
authors:
  item: Erskine PT
  item: Norton E
  item: Cooper JB
  item: Lambert R
  item: Coker A
  item: Lewis G
  item: Spencer P
  item: Sarwar M
  item: Wood SP
  item: Warren MJ
  item: Shoolingin-Jordan PM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P15002

Production, purification, and characterization of a Mg2+-responsive porphobilinogen synthase from Pseudomonas aeruginosa.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10529243
journal: Biochemistry
volume: 38
pages: 13968-75
published year: 1999
authors:
  item: Frankenberg N
  item: Heinz DW
  item: Jahn D

Pseudomonas aeruginosa contains a novel type V porphobilinogen synthase with no required catalytic metal ions.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10529244
journal: Biochemistry
volume: 38
pages: 13976-82
published year: 1999
authors:
  item: Frankenberg N
  item: Jahn D
  item: Jaffe EK

High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS).
medline id: 99286289
references: http://www.ncbi.nlm.nih.gov/pubmed/10356331
journal: J Mol Biol
volume: 289
pages: 591-602
published year: 1999
authors:
  item: Frankenberg N
  item: Erskine PT
  item: Cooper JB
  item: Shoolingin-Jordan PM
  item: Jahn D
  item: Heinz DW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q59643

The Schiff base complex of yeast 5-aminolaevulinic acid dehydratase with laevulinic acid.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
medline id: 99313446
references: http://www.ncbi.nlm.nih.gov/pubmed/10386874
journal: Protein Sci
volume: 8
pages: 1250-6
published year: 1999
authors:
  item: Erskine PT
  item: Newbold R
  item: Roper J
  item: Coker A
  item: Warren MJ
  item: Shoolingin-Jordan PM
  item: Wood SP
  item: Cooper JB
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P05373

MAD analyses of yeast 5-aminolaevulinate dehydratase: their use in structure determination and in defining the metal-binding sites.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
medline id: 20207114
references: http://www.ncbi.nlm.nih.gov/pubmed/10739915
journal: Acta Crystallogr D Biol Crystallogr
volume: 56
pages: 421-30
published year: 2000
authors:
  item: Erskine PT
  item: Duke EM
  item: Tickle IJ
  item: Senior NM
  item: Warren MJ
  item: Cooper JB
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P05373

Porphobilinogen synthase from pea: expression from an artificial gene, kinetic characterization, and novel implications for subunit interactions.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10913315
journal: Biochemistry
volume: 39
pages: 9018-29
published year: 2000
authors:
  item: Kervinen J
  item: Dunbrack RL Jr
  item: Litwin S
  item: Martins J
  item: Scarrow RC
  item: Volin M
  item: Yeung AT
  item: Yoon E
  item: Jaffe EK

Inhibition of Escherichia coli porphobilinogen synthase using analogs of postulated intermediates.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10712932
journal: Chem Biol
volume: 7
pages: 185-96
published year: 2000
authors:
  item: Jarret C
  item: Stauffer F
  item: Henz ME
  item: Marty M
  item: Luond RM
  item: Bobalova J
  item: Schurmann P
  item: Neier R

Mechanistic basis for suicide inactivation of porphobilinogen synthase by 4,7-dioxosebacic acid, an inhibitor that shows dramatic species selectivity.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
medline id: 21338255
references: http://www.ncbi.nlm.nih.gov/pubmed/11444968
journal: Biochemistry
volume: 40
pages: 8227-36
published year: 2001
authors:
  item: Kervinen J
  item: Jaffe EK
  item: Stauffer F
  item: Neier R
  item: Wlodawer A
  item: Zdanov A
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P15002

The X-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with two diacid inhibitors.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
medline id: 21405508
references: http://www.ncbi.nlm.nih.gov/pubmed/11513881
journal: FEBS Lett
volume: 503
pages: 196-200
published year: 2001
authors:
  item: Erskine PT
  item: Coates L
  item: Newbold R
  item: Brindley AA
  item: Stauffer F
  item: Wood SP
  item: Warren MJ
  item: Cooper JB
  item: Shoolingin-Jordan PM
  item: Neier R
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P05373

Mechanistic implications of mutations to the active site lysine of porphobilinogen synthase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11032841
journal: J Biol Chem
volume: 276
pages: 1538-44
published year: 2001
authors:
  item: Mitchell LW
  item: Volin M
  item: Martins J
  item: Jaffe EK

The x-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with substrate and three inhibitors.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
medline id: 21431818
references: http://www.ncbi.nlm.nih.gov/pubmed/11545591
journal: J Mol Biol
volume: 312
pages: 133-41
published year: 2001
authors:
  item: Erskine PT
  item: Newbold R
  item: Brindley AA
  item: Wood SP
  item: Shoolingin-Jordan PM
  item: Warren MJ
  item: Cooper JB
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P05373

Selenoxides inhibit delta-aminolevulinic acid dehydratase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11275419
journal: Toxicol Lett
volume: 119
pages: 27-37
published year: 2001
authors:
  item: Farina M
  item: Folmer V
  item: Bolzan RC
  item: Andrade LH
  item: Zeni G
  item: Braga AL
  item: Rocha JB

5-Aminolaevulinic acid dehydratase: metals, mutants and mechanism.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12196142
journal: Biochem Soc Trans
volume: 30
pages: 584-90
published year: 2002
authors:
  item: Shoolingin-Jordan PM
  item: Spencer P
  item: Sarwar M
  item: Erskine PE
  item: Cheung KM
  item: Cooper JB
  item: Norton EB

Species-specific inhibition of porphobilinogen synthase by 4-oxosebacic acid.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
medline id: 22028088
references: http://www.ncbi.nlm.nih.gov/pubmed/11909869
journal: J Biol Chem
volume: 277
pages: 19792-9
published year: 2002
authors:
  item: Jaffe EK
  item: Kervinen J
  item: Martins J
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references: P15002

Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12079382
journal: J Mol Biol
volume: 320
pages: 237-47
published year: 2002
authors:
  item: Frere F
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  item: Jahn D
  item: Heinz DW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

X-ray structure of a putative reaction intermediate of 5-aminolaevulinic acid dehydratase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF MUTANT D139N.
medline id: 22075365
references: http://www.ncbi.nlm.nih.gov/pubmed/12777167
journal: Biochem J
volume: 373
pages: 733-8
published year: 2003
authors:
  item: Erskine PT
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  item: Warren MJ
  item: Shoolingin-Jordan PM
  item: Cooper JB
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q59643

Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12897770
journal: Nat Struct Biol
volume: 10
pages: 757-63
published year: 2003
authors:
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  item: Stith L
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  item: Zdanov A
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references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The X-ray structure of the plant like 5-aminolaevulinic acid dehydratase from Chlorobium vibrioforme complexed with the inhibitor laevulinic acid at 2.6 A resolution.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15327955
journal: J Mol Biol
volume: 342
pages: 563-70
published year: 2004
authors:
  item: Coates L
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  item: Erskine PT
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  item: Avissar YJ
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  item: Mohammed F
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  item: Cooper JB
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Tracking the evolution of porphobilinogen synthase metal dependence in vitro.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15644204
journal: J Mol Biol
volume: 345
pages: 1059-70
published year: 2005
authors:
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references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16131755
journal: Acta Crystallogr D Biol Crystallogr
volume: 61
pages: 1222-6
published year: 2005
authors:
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  item: Coates L
  item: Newbold R
  item: Brindley AA
  item: Stauffer F
  item: Beaven GD
  item: Gill R
  item: Coker A
  item: Wood SP
  item: Warren MJ
  item: Shoolingin-Jordan PM
  item: Neier R
  item: Cooper JB
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structure of Chlorobium vibrioforme 5-aminolaevulinic acid dehydratase complexed with a diacid inhibitor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16304458
journal: Acta Crystallogr D Biol Crystallogr
volume: 61
pages: 1594-8
published year: 2005
authors:
  item: Coates L
  item: Beaven G
  item: Erskine PT
  item: Beale SI
  item: Wood SP
  item: Shoolingin-Jordan PM
  item: Cooper JB
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Probing the active site of Pseudomonas aeruginosa porphobilinogen synthase using newly developed inhibitors.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16819823
journal: Biochemistry
volume: 45
pages: 8243-53
published year: 2006
authors:
  item: Frere F
  item: Nentwich M
  item: Gacond S
  item: Heinz DW
  item: Neier R
  item: Frankenberg-Dinkel N
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

IntermediateAnalogue
pdb: 1w1zB
ligand het code: LEA

IntermediateAnalogue
pdb: 2c1hA
ligand het code: DSB

IntermediateAnalogue
pdb: 2c1hB
ligand het code: DSB

ReferenceForCatalyticMechanism
reference index: 1
reference section: Scheme 2, p.285
reference step: 5

ReferenceForCatalyticMechanism
reference index: 5
reference section: Fig.1, p.8346

ReferenceForCatalyticMechanism
reference index: 7
reference section: Fig.7, p.2122

ReferenceForCatalyticMechanism
reference index: 11
reference section: Fig.1, Fig.2, p.11561

ReferenceForCatalyticMechanism
reference index: 13
reference section: Fig.3, p.169-175
reference step: 2

ReferenceForCatalyticMechanism
reference index: 17
reference section: p.1027

ReferenceForCatalyticMechanism
reference index: 20
reference section: Fig.7, p.4273-4275

ReferenceForCatalyticMechanism
reference index: 23
reference section: Fig.1, p.599

ReferenceForCatalyticMechanism
reference index: 24
reference section: Fig.6, p.1254

ReferenceForCatalyticMechanism
reference index: 25
reference section: p.428

ReferenceForCatalyticMechanism
reference index: 27
reference section: Fig.8, p.191-194
reference step: 11

ReferenceForCatalyticMechanism
reference index: 28
reference section: p.8234-8256

ReferenceForCatalyticMechanism
reference index: 29
reference section: Fig.4, p.199-200
reference step: 8

ReferenceForCatalyticMechanism
reference index: 31
reference section: p.138-139

ReferenceForCatalyticMechanism
reference index: 33
reference section: Scheme 2, p.589-590
reference step: 7

ReferenceForCatalyticMechanism
reference index: 34
reference section: p.19797-19798

ReferenceForCatalyticMechanism
reference index: 35
reference section: Fig.6, p.243-245
reference step: 10

ReferenceForCatalyticMechanism
reference index: 36
reference section: Scheme 2, p.736-737
reference step: 8

ReferenceForCatalyticMechanism
reference index: 38
reference section: p.567-568

ReferenceForCatalyticMechanism
reference index: 41
reference section: p.1225-1226

ReferenceForCatalyticMechanism
reference index: 42
reference section: Fig.5, p.8251-8252