T00108
type: Enzyme
cath: Rossmann fold
cath: D-amino Acid Aminotransferase; Chain A, domain 1
cath: Dna Ligase; domain 1
ec: https://purl.uniprot.org/enzyme/6.3.2.4
csa: 2dln
uniprot: P07862
uniprot: P71454
kegg enzyme: D-alanine---D-alanine ligase
kegg enzyme: MurE synthetase [ambiguous]
kegg enzyme: alanine:alanine ligase (ADP-forming)
kegg enzyme: alanylalanine synthetase
kegg pathway: D-Alanine metabolism
kegg pathway: Peptidoglycan biosynthesis
kegg cofactor: Magnesium
kegg substrate: ATP
kegg substrate: D-Alanine
kegg product: ADP
kegg product: Orthophosphate
kegg product: D-Alanyl-D-alanine
kegg intermediate: D-alanyl acylphosphate
pdb: 1ehiA01
pdb: 1ehiB01
pdb: 1iovA01
pdb: 1iowA01
pdb: 2dlnA01
pdb: 1ehiA02
pdb: 1ehiB02
pdb: 1iovA02
pdb: 1iowA02
pdb: 2dlnA02
pdb: 1ehiA03
pdb: 1ehiB03
pdb: 1iovA03
pdb: 1iowA03
pdb: 2dlnA03
pdb bound state: Unbound
  compound: ATP
  pdb: 1ehiA01
pdb bound state: Unbound
  compound: ATP
  pdb: 1ehiB01
pdb bound state: Unbound
  compound: ATP
  pdb: 1iovA01
pdb bound state: Unbound
  compound: ATP
  pdb: 1iowA01
pdb bound state: Unbound
  compound: ATP
  pdb: 2dlnA01
pdb bound state: Unbound
  compound: ATP
  pdb: 1ehiA02
pdb bound state: Unbound
  compound: ATP
  pdb: 1ehiB02
pdb bound state: Unbound
  compound: ATP
  pdb: 1iovA02
pdb bound state: Unbound
  compound: ATP
  pdb: 1iowA02
pdb bound state: Unbound
  compound: ATP
  pdb: 2dlnA02
active site residues resources: Active site mapping of Escherichia coli D-Ala-D-Ala ligase by structure-based mutagenesis.
active site residues resources: A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:d-alanine ligase of Escherichia coli.
active site residues resources: D-Alanyl-D-lactate and D-alanyl-D-alanine synthesis by D-alanyl-D-alanine ligase from vancomycin-resistant Leuconostoc mesenteroides. Effects of a phenylalanine 261 to tyrosine mutation.
active site residues resources: P07862
active site residues resources: 1iov
active site residues resources: 1iow
active site residues resources: 2dln
references: ATP-dependent inactivation and slow binding inhibition of Salmonella typhimurium D-alanine:D-alanine ligase (ADP) by (aminoalkyl)phosphinate and aminophosphonate analogues of D-alanine.
references: Synthesis of an analogue of tabtoxinine as a potential inhibitor of D-alanine:D-alanine ligase (ADP forming).
references: D-alanine-D-alanine ligase (ADP) from Salmonella typhimurium. Overproduction, purification, crystallization and preliminary X-ray analysis.
references: Rotational resonance determination of the structure of an enzyme-inhibitor complex: phosphorylation of an (aminoalkyl)phosphinate inhibitor of D-alanyl-D-alanine ligase by ATP.
references: Sequence of a putative glutathione synthetase II gene and flanking regions from Anaplasma centrale.
references: Identification of a common protease-sensitive region in D-alanyl-D-alanine and D-alanyl-D-lactate ligases and photoaffinity labeling with 8-azido ATP.
references: Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution.
references: Active site mapping of Escherichia coli D-Ala-D-Ala ligase by structure-based mutagenesis.
references: A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:d-alanine ligase of Escherichia coli.
references: Gain of D-alanyl-D-lactate or D-lactyl-D-alanine synthetase activities in three active-site mutants of the Escherichia coli D-alanyl-D-alanine ligase B.
references: Evolution of structure and substrate specificity in D-alanine:D-alanine ligases and related enzymes.
references: Biotin carboxylase comes into the fold.
references: Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins.
references: D-alanine:D-alanine ligase: phosphonate and phosphinate intermediates with wild type and the Y216F mutant.
references: D-Alanyl-D-lactate and D-alanyl-D-alanine synthesis by D-alanyl-D-alanine ligase from vancomycin-resistant Leuconostoc mesenteroides. Effects of a phenylalanine 261 to tyrosine mutation.
references: Synapsin I is structurally similar to ATP-utilizing enzymes.
references: Enzyme-mononucleotide interactions: three different folds share common structural elements for ATP recognition.
references: Two "unrelated" families of ATP-dependent enzymes share extensive structural similarities about their cofactor binding sites.
references: The structure of SAICAR synthase: an enzyme in the de novo pathway of purine nucleotide biosynthesis.
references: Mutational analysis of active-site residues of the enterococcal D-ala-D-Ala dipeptidase VanX and comparison with Escherichia coli D-ala-D-Ala ligase and D-ala-D-Ala carboxypeptidase VanY.
references: Structural motif of phosphate-binding site common to various protein superfamilies: all-against-all structural comparison of protein-mononucleotide complexes.
references: D-Ala-D-X ligases: evaluation of D-alanyl phosphate intermediate by MIX, PIX and rapid quench studies.
references: Modeling of Enterococcus faecalis D-alanine:D-alanine ligase: structure-based study of the active site in the wild-type enzyme and in glycopeptide-dependent mutants.
references: When fold is not important: a common structural framework for adenine and AMP binding in 12 unrelated protein families.
references: Enzymes of vancomycin resistance: the structure of D-alanine-D-lactate ligase of naturally resistant Leuconostoc mesenteroides.
references: Sequencing of the ddl gene and modeling of the mutated D-alanine:D-alanine ligase in glycopeptide-dependent strains of Enterococcus faecium.
comment: This enzyme is homologous to Glutathione synthetase (Swiss-prot;P04425, T00107 in EzCatDB). This enzyme catalyzes the following reactions (see [7], [8]): (A) Transfer of phosphate group from ATP to carboxyl oxygen of D-alanine, forming an intermediate, D-alanyl acylphosphate: (B) Transfer of acyl group from D-alanyl acylphosphate to amine group of the second D-alanine substrate, releasing inorganic phosphate:

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.20
catalytic domain: index.html

D-amino Acid Aminotransferase; Chain A, domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.470.20
catalytic domain: index.html

Dna Ligase; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.1490.20
catalytic domain: index.html

D-Alanine metabolism
type: KeggPathway
references: KEGG:MAP00473

Peptidoglycan biosynthesis
type: KeggPathway
references: KEGG:MAP00550

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

ATP
type: KeggSubstrate
references: KEGG:C00002
compound type: amine group
compound type: nucleotide
references: CHEBI:15422
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

D-Alanine
type: KeggSubstrate
references: KEGG:C00133
compound type: amino acids
references: CHEBI:15570
references: CHEBI:57416
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

ADP
type: KeggProduct
references: KEGG:C00008
compound type: amine group
compound type: nucleotide
references: CHEBI:16761
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Orthophosphate
type: KeggProduct
references: KEGG:C00009
compound type: phosphate group/phosphate ion
references: CHEBI:26078
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

D-Alanyl-D-alanine
type: KeggProduct
references: KEGG:C00993
compound type: amino acids
compound type: amide group
compound type: amine group
compound type: carboxyl group
references: CHEBI:16576
references: CHEBI:57822
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

D-alanyl acylphosphate
type: KeggIntermediate
references: KEGG:C12021

1ehiA01
type: Pdb
references: 1ehi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ehi
catalytic residue: GLU 16

1ehiB01
type: Pdb
references: 1ehi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ehi
catalytic residue: GLU 416

1iovA01
type: Pdb
references: 1iov
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iov
catalytic residue: GLU 15

1iowA01
type: Pdb
references: 1iow
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iow
catalytic residue: GLU 15

2dlnA01
type: Pdb
references: 2dln
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2dln
catalytic residue: GLU 15

1ehiA02
type: Pdb
references: 1ehi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ehi
catalytic residue: LYS 260; ;ARG 301
cofactor binding residue: ASP 303(Magnesium-1);GLU 316(Magnesium-1 & -2);ASN 318(Magnesium-2)
main chain in catalysis: GLY 322

1ehiB02
type: Pdb
references: 1ehi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ehi
catalytic residue: ; ;ARG 701
cofactor binding residue: ASP 703(Magnesium-1);GLU 716(Magnesium-1 & -2);ASN 718(Magnesium-2)
main chain in catalysis: GLY 722
comment: invisible 645-666

1iovA02
type: Pdb
references: 1iov
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iov
catalytic residue: LYS 215;TYR 216;ARG 255
cofactor binding residue: ASP 257(Magnesium-1);GLU 270(Magnesium-1 & -2);ASN 272(Magnesium-2)
main chain in catalysis: GLY 276

1iowA02
type: Pdb
references: 1iow
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iow
catalytic residue: LYS 215; ;ARG 255
cofactor binding residue: ASP 257(Magnesium-1);GLU 270(Magnesium-1 & -2);ASN 272(Magnesium-2)
main chain in catalysis: GLY 276
comment: mutant Y216F

2dlnA02
type: Pdb
references: 2dln
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2dln
catalytic residue: LYS 215;TYR 216;ARG 255
cofactor binding residue: ASP 257(Magnesium-1);GLU 270(Magnesium-1 & -2);ASN 272(Magnesium-2)
main chain in catalysis: GLY 276

1ehiA03
type: Pdb
references: 1ehi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ehi
catalytic residue: SER 186

1ehiB03
type: Pdb
references: 1ehi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ehi
catalytic residue: SER 586

1iovA03
type: Pdb
references: 1iov
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iov
catalytic residue: SER 150

1iowA03
type: Pdb
references: 1iow
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iow
catalytic residue: SER 150

2dlnA03
type: Pdb
references: 2dln
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2dln
catalytic residue: SER 150

ATP-dependent inactivation and slow binding inhibition of Salmonella typhimurium D-alanine:D-alanine ligase (ADP) by (aminoalkyl)phosphinate and aminophosphonate analogues of D-alanine.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3044448
journal: Biochemistry
volume: 27
pages: 3709-14
published year: 1988
authors:
  item: Duncan K
  item: Walsh CT

Synthesis of an analogue of tabtoxinine as a potential inhibitor of D-alanine:D-alanine ligase (ADP forming).
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2562853
journal: J Med Chem
volume: 32
pages: 165-70
published year: 1989
authors:
  item: Greenlee WJ
  item: Springer JP
  item: Patchett AA

D-alanine-D-alanine ligase (ADP) from Salmonella typhimurium. Overproduction, purification, crystallization and preliminary X-ray analysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2648004
journal: J Mol Biol
volume: 205
pages: 461-3
published year: 1989
authors:
  item: Knox JR
  item: Liu HS
  item: Walsh CT
  item: Zawadzke LE

Rotational resonance determination of the structure of an enzyme-inhibitor complex: phosphorylation of an (aminoalkyl)phosphinate inhibitor of D-alanyl-D-alanine ligase by ATP.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2200515
journal: Biochemistry
volume: 29
pages: 5767-75
published year: 1990
authors:
  item: McDermott AE
  item: Creuzet F
  item: Griffin RG
  item: Zawadzke LE
  item: Ye QZ
  item: Walsh CT

Sequence of a putative glutathione synthetase II gene and flanking regions from Anaplasma centrale.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1540152
journal: Biochem Biophys Res Commun
volume: 182
pages: 1040-6
published year: 1992
authors:
  item: Peters JM
  item: Dalrymple BP
  item: Jorgensen WK

Identification of a common protease-sensitive region in D-alanyl-D-alanine and D-alanyl-D-lactate ligases and photoaffinity labeling with 8-azido ATP.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8251948
journal: Protein Sci
volume: 2
pages: 1765-9
published year: 1993
authors:
  item: Wright GD
  item: Walsh CT

Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
medline id: 95025939
references: http://www.ncbi.nlm.nih.gov/pubmed/7939684
journal: Science
volume: 266
pages: 439-43
published year: 1994
authors:
  item: Fan C
  item: Moews PC
  item: Walsh CT
  item: Knox JR
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P07862

Active site mapping of Escherichia coli D-Ala-D-Ala ligase by structure-based mutagenesis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7893688
journal: Biochemistry
volume: 34
pages: 2768-76
published year: 1995
authors:
  item: Shi Y
  item: Walsh CT

A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:d-alanine ligase of Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7862655
journal: Proc Natl Acad Sci U S A
volume: 92
pages: 1172-6
published year: 1995
authors:
  item: Fan C
  item: Moews PC
  item: Shi Y
  item: Walsh CT
  item: Knox JR

Gain of D-alanyl-D-lactate or D-lactyl-D-alanine synthetase activities in three active-site mutants of the Escherichia coli D-alanyl-D-alanine ligase B.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8756703
journal: Biochemistry
volume: 35
pages: 10464-71
published year: 1996
authors:
  item: Park IS
  item: Lin CH
  item: Walsh CT

Evolution of structure and substrate specificity in D-alanine:D-alanine ligases and related enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8662022
journal: J Mol Evol
volume: 42
pages: 706-12
published year: 1996
authors:
  item: Evers S
  item: Casadewall B
  item: Charles M
  item: Dutka-Malen S
  item: Galimand M
  item: Courvalin P

Biotin carboxylase comes into the fold.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8564538
journal: Nat Struct Biol
volume: 3
pages: 128-32
published year: 1996
authors:
  item: Artymiuk PJ
  item: Poirrette AR
  item: Rice DW
  item: Willett P

Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9010922
journal: Protein Eng
volume: 9
pages: 1083-92
published year: 1996
authors:
  item: Matsuda K
  item: Mizuguchi K
  item: Nishioka T
  item: Kato H
  item: Go N
  item: Oda J

D-alanine:D-alanine ligase: phosphonate and phosphinate intermediates with wild type and the Y216F mutant.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
medline id: 97207065
references: http://www.ncbi.nlm.nih.gov/pubmed/9054558
journal: Biochemistry
volume: 36
pages: 2531-8
published year: 1997
authors:
  item: Fan C
  item: Park IS
  item: Walsh CT
  item: Knox JR
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P07862

D-Alanyl-D-lactate and D-alanyl-D-alanine synthesis by D-alanyl-D-alanine ligase from vancomycin-resistant Leuconostoc mesenteroides. Effects of a phenylalanine 261 to tyrosine mutation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9083053
journal: J Biol Chem
volume: 272
pages: 9210-4
published year: 1997
authors:
  item: Park IS
  item: Walsh CT

Synapsin I is structurally similar to ATP-utilizing enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9463376
journal: EMBO J
volume: 17
pages: 977-84
published year: 1998
authors:
  item: Esser L
  item: Wang CR
  item: Hosaka M
  item: Smagula CS
  item: Sudhof TC
  item: Deisenhofer J

Enzyme-mononucleotide interactions: three different folds share common structural elements for ATP recognition.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10082373
journal: Protein Sci
volume: 7
pages: 1768-71
published year: 1998
authors:
  item: Denessiouk KA
  item: Lehtonen JV
  item: Johnson MS

Two "unrelated" families of ATP-dependent enzymes share extensive structural similarities about their cofactor binding sites.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9605318
journal: Protein Sci
volume: 7
pages: 1136-46
published year: 1998
authors:
  item: Denessiouk KA
  item: Lehtonen JV
  item: Korpela T
  item: Johnson MS

The structure of SAICAR synthase: an enzyme in the de novo pathway of purine nucleotide biosynthesis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9551557
journal: Structure
volume: 6
pages: 363-76
published year: 1998
authors:
  item: Levdikov VM
  item: Barynin VV
  item: Grebenko AI
  item: Melik-Adamyan WR
  item: Lamzin VS
  item: Wilson KS

Mutational analysis of active-site residues of the enterococcal D-ala-D-Ala dipeptidase VanX and comparison with Escherichia coli D-ala-D-Ala ligase and D-ala-D-Ala carboxypeptidase VanY.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10074467
journal: Chem Biol
volume: 6
pages: 177-87
published year: 1999
authors:
  item: Lessard IA
  item: Walsh CT

Structural motif of phosphate-binding site common to various protein superfamilies: all-against-all structural comparison of protein-mononucleotide complexes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10065705
journal: Protein Eng
volume: 12
pages: 11-4
published year: 1999
authors:
  item: Kinoshita K
  item: Sadanami K
  item: Kidera A
  item: Go N

D-Ala-D-X ligases: evaluation of D-alanyl phosphate intermediate by MIX, PIX and rapid quench studies.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10903933
journal: Chem Biol
volume: 7
pages: 505-14
published year: 2000
authors:
  item: Healy VL
  item: Mullins LS
  item: Li X
  item: Hall SE
  item: Raushel FM
  item: Walsh CT

Modeling of Enterococcus faecalis D-alanine:D-alanine ligase: structure-based study of the active site in the wild-type enzyme and in glycopeptide-dependent mutants.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10937441
journal: J Mol Microbiol Biotechnol
volume: 2
pages: 321-30
published year: 2000
authors:
  item: Prevost M
  item: Van Belle D
  item: Tulkens PM
  item: Courvalin P
  item: Van Bambeke F

When fold is not important: a common structural framework for adenine and AMP binding in 12 unrelated protein families.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10713991
journal: Proteins
volume: 38
pages: 310-26
published year: 2000
authors:
  item: Denessiouk KA
  item: Johnson MS

Enzymes of vancomycin resistance: the structure of D-alanine-D-lactate ligase of naturally resistant Leuconostoc mesenteroides.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10801495
journal: Structure Fold Des
volume: 8
pages: 463-70
published year: 2000
authors:
  item: Kuzin AP
  item: Sun T
  item: Jorczak-Baillass J
  item: Healy VL
  item: Walsh CT
  item: Knox JR
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Sequencing of the ddl gene and modeling of the mutated D-alanine:D-alanine ligase in glycopeptide-dependent strains of Enterococcus faecium.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11274474
journal: Protein Sci
volume: 10
pages: 836-44
published year: 2001
authors:
  item: Gholizadeh Y
  item: Prevost M
  item: Van Bambeke F
  item: Casadewall B
  item: Tulkens PM
  item: Courvalin P

Analogue
pdb: 1ehiA02
ligand het code: PHY

Analogue
pdb: 1iovA02
ligand het code: POB

Analogue
pdb: 1iowA02
ligand het code: PHY

Analogue
pdb: 2dlnA02
ligand het code: PHY

ReferenceForCatalyticMechanism
reference index: 1
reference section: Fig.4, Fig.5, p.3714

ReferenceForCatalyticMechanism
reference index: 2
reference section: Scheme II

ReferenceForCatalyticMechanism
reference index: 4
reference section: Fig.1, p.5774

ReferenceForCatalyticMechanism
reference index: 7
reference section: Fig.5, Fig.6, p.441
reference step: 3

ReferenceForCatalyticMechanism
reference index: 8
reference section: Scheme 1, Scheme 2, p.2773-2776
reference step: 4

ReferenceForCatalyticMechanism
reference index: 9
reference section: Scheme I
reference step: 3

ReferenceForCatalyticMechanism
reference index: 10
reference section: Eq.(11), Eq.(12), p.10469-10470

ReferenceForCatalyticMechanism
reference index: 14
reference section: p.2536-2537

ReferenceForCatalyticMechanism
reference index: 15

ReferenceForCatalyticMechanism
reference index: 25
reference section: Fig.1, p.466, p.467-468
reference step: 2