S00232
type: Enzyme
rlcp: p458
rlcp: p453
cath: TIM Barrel
ec: https://purl.uniprot.org/enzyme/3.5.4.4
csa: 1a4l
uniprot: P03958
uniprot: P56658
kegg enzyme: adenosine deaminase
kegg pathway: Purine metabolism
kegg cofactor: Zinc
kegg substrate: Adenosine
kegg substrate: H2O
kegg product: Inosine
kegg product: NH3
kegg intermediate: 6-Hydroxy-adenosine
pdb: 1a4lA
pdb: 1a4lB
pdb: 1a4lC
pdb: 1a4lD
pdb: 1a4mA
pdb: 1a4mB
pdb: 1a4mC
pdb: 1a4mD
pdb: 1addA
pdb: 1fkwA
pdb: 1fkxA
pdb: 1uioA
pdb: 1uipA
pdb: 2adaA
pdb: 1krmA
pdb: 1ndvA
pdb: 1ndwA
pdb: 1ndyA
pdb: 1ndzA
pdb: 1o5rA
pdb: 1qxlA
pdb: 1umlA
pdb: 1v78A
pdb: 1v79A
pdb: 1v7aA
pdb: 1w1iE
pdb: 1w1iF
pdb: 1w1iG
pdb: 1w1iH
pdb: 2bgnE
pdb: 2bgnF
pdb: 2bgnG
pdb: 2bgnH
active site residues resources: Crystallographic observation of a trapped tetrahedral intermediate in a metalloenzyme.
active site residues resources: Enzyme-substrate complexes of adenosine and cytidine deaminases: absence of accumulation of water adducts.
active site residues resources: Site-directed mutagenesis of histidine 238 in mouse adenosine deaminase: substitution of histidine 238 does not impede hydroxylate formation.
active site residues resources: Functional residues at the active site of bovine brain adenosine deaminase.
active site residues resources: Structure-based de novo design of non-nucleoside adenosine deaminase inhibitors.
references: Functional residues at the active site of bovine brain adenosine deaminase.
references: Adenosine deaminase converts purine riboside into an analogue of a reactive intermediate: a 13C NMR and kinetic study.
references: Evidence from nitrogen-15 and solvent deuterium isotope effects on the chemical mechanism of adenosine deaminase.
references: Preliminary X-ray analysis of crystals of murine adenosine deaminase.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/S00232#4
references: Structural and conformational analysis of pentostatin (2'-deoxycoformycin), a potent inhibitor of adenosine deaminase.
references: Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations.
references: A transition state in pieces: major contributions of entropic effects to ligand binding by adenosine deaminase.
references: The rate of formation of transition-state analogues in the active site of adenosine deaminase is encounter-controlled: implications for the mechanism.
references: Refined 2.5 A structure of murine adenosine deaminase at pH 6.0.
references: A pre-transition-state mimic of an enzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water.
references: Crystallographic observation of a trapped tetrahedral intermediate in a metalloenzyme.
references: Site-directed mutagenesis of active site glutamate-217 in mouse adenosine deaminase.
references: Enzyme-substrate complexes of adenosine and cytidine deaminases: absence of accumulation of water adducts.
references: Probing the functional role of two conserved active site aspartates in mouse adenosine deaminase.
references: Site-directed mutagenesis of histidine 238 in mouse adenosine deaminase: substitution of histidine 238 does not impede hydroxylate formation.
references: An adenosine deaminase (ADA) allele contains two newly identified deleterious mutations (Y97C and L106V) that interact to abolish enzyme activity.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/S00232#18
references: Characterization of hydrogen bonding in the complex of adenosine deaminase with a transition state analogue: a Raman spectroscopic study.
references: Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH of maximum activity.
references: Probing the active site of adenosine deaminase by a pH responsive fluorescent competitive inhibitor.
references: Adenosine deaminase prefers a distinct sugar ring conformation for binding and catalysis: kinetic and structural studies.
references: 3'-Beta-ethynyl and 2'-deoxy-3'-beta-ethynyl adenosines: first 3'-beta-branched-adenosines substrates of adenosine deaminase.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/S00232#24
references: Clustered charged amino acids of human adenosine deaminase comprise a functional epitope for binding the adenosine deaminase complexing protein CD26/dipeptidyl peptidase IV.
references: The stability curve of bovine adenosine deaminase is bimodal.

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

Purine metabolism
type: KeggPathway
references: KEGG:MAP00230

Zinc
type: KeggCofactor
references: KEGG:C00038
references: CHEBI:29105
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: heavy metal

Adenosine
type: KeggSubstrate
references: KEGG:C00212
references: CHEBI:16335
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: amine group
compound type: nucleoside

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

Inosine
type: KeggProduct
references: KEGG:C00294
references: CHEBI:17596
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: amide group
compound type: nucleoside

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

6-Hydroxy-adenosine
type: KeggIntermediate
references: KEGG:I00018

1a4lA
type: Pdb
references: 1a4l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a4l
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

1a4lB
type: Pdb
references: 1a4l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a4l
catalytic residue: GLU 717;HIS 738;ASP 795
cofactor binding residue: HIS 515;HIS 517;HIS 714;ASP 795(Zinc binding)

1a4lC
type: Pdb
references: 1a4l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a4l
catalytic residue: GLU 1217;HIS 1238;ASP 1295
cofactor binding residue: HIS 1015;HIS 1017;HIS 1214;ASP 1295(Zinc binding)

1a4lD
type: Pdb
references: 1a4l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a4l
catalytic residue: GLU 1717;HIS 1738;ASP 1795
cofactor binding residue: HIS 1515;HIS 1517;HIS 1714;ASP 1795(Zinc binding)

1a4mA
type: Pdb
references: 1a4m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a4m
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

1a4mB
type: Pdb
references: 1a4m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a4m
catalytic residue: GLU 717;HIS 738;ASP 795
cofactor binding residue: HIS 515;HIS 517;HIS 714;ASP 795(Zinc binding)

1a4mC
type: Pdb
references: 1a4m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a4m
catalytic residue: GLU 1217;HIS 1238;ASP 1295
cofactor binding residue: HIS 1015;HIS 1017;HIS 1214;ASP 1295(Zinc binding)

1a4mD
type: Pdb
references: 1a4m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a4m
catalytic residue: GLU 1717;HIS 1738;ASP 1795
cofactor binding residue: HIS 1515;HIS 1517;HIS 1714;ASP 1795(Zinc binding)

1addA
type: Pdb
references: 1add
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1add
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

1fkwA
type: Pdb
references: 1fkw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fkw
catalytic residue: GLU 217;HIS 238;
cofactor binding residue: HIS 15;HIS 17;HIS 214; (Zinc binding)
comment: mutant D295E

1fkxA
type: Pdb
references: 1fkx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fkx
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)
comment: mutant D296A

1uioA
type: Pdb
references: 1uio
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1uio
catalytic residue: GLU 217; ;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)
comment: mutant H238A

1uipA
type: Pdb
references: 1uip
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1uip
catalytic residue: GLU 217; ;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)
comment: mutant H238E

2adaA
type: Pdb
references: 2ada
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ada
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

1krmA
type: Pdb
references: 1krm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1krm
catalytic residue: GLU 214;HIS 235;ASP 292
cofactor binding residue: HIS 12;HIS 14;HIS 211;ASP 292(Zinc binding)

1ndvA
type: Pdb
references: 1ndv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ndv
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

1ndwA
type: Pdb
references: 1ndw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ndw
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

1ndyA
type: Pdb
references: 1ndy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ndy
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

1ndzA
type: Pdb
references: 1ndz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ndz
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

1o5rA
type: Pdb
references: 1o5r
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1o5r
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

1qxlA
type: Pdb
references: 1qxl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qxl
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

1umlA
type: Pdb
references: 1uml
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1uml
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

1v78A
type: Pdb
references: 1v78
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1v78
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

1v79A
type: Pdb
references: 1v79
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1v79
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

1v7aA
type: Pdb
references: 1v7a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1v7a
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

1w1iE
type: Pdb
references: 1w1i
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1w1i
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

1w1iF
type: Pdb
references: 1w1i
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1w1i
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

1w1iG
type: Pdb
references: 1w1i
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1w1i
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

1w1iH
type: Pdb
references: 1w1i
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1w1i
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

2bgnE
type: Pdb
references: 2bgn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bgn
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

2bgnF
type: Pdb
references: 2bgn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bgn
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

2bgnG
type: Pdb
references: 2bgn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bgn
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

2bgnH
type: Pdb
references: 2bgn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bgn
catalytic residue: GLU 217;HIS 238;ASP 295
cofactor binding residue: HIS 15;HIS 17;HIS 214;ASP 295(Zinc binding)

Crystallographic observation of a trapped tetrahedral intermediate in a metalloenzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7634072
journal: Nat Struct Biol
volume: 1
pages: 691-4
published year: 1994
authors:
  item: Wilson DK
  item: Quiocho FA

Enzyme-substrate complexes of adenosine and cytidine deaminases: absence of accumulation of water adducts.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8664259
journal: Biochemistry
volume: 35
pages: 4697-703
published year: 1996
authors:
  item: Shih P
  item: Wolfenden R

Site-directed mutagenesis of histidine 238 in mouse adenosine deaminase: substitution of histidine 238 does not impede hydroxylate formation.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
medline id: 97098127
references: http://www.ncbi.nlm.nih.gov/pubmed/8942668
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P03958
journal: Biochemistry
volume: 35
pages: 15019-28
published year: 1996
authors:
  item: Sideraki V
  item: Wilson DK
  item: Kurz LC
  item: Quiocho FA
  item: Rudolph FB

Functional residues at the active site of bovine brain adenosine deaminase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9442929
journal: Biochem Mol Biol Int
volume: 43
pages: 1339-52
published year: 1997
authors:
  item: Lupidi G
  item: Marmocchi F
  item: Venardi G
  item: Cristalli G

Structure-based de novo design of non-nucleoside adenosine deaminase inhibitors.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12643924
journal: Bioorg Med Chem Lett
volume: 13
pages: 1115-8
published year: 2003
authors:
  item: Terasaka T
  item: Nakanishi I
  item: Nakamura K
  item: Eikyu Y
  item: Kinoshita T
  item: Nishio N
  item: Sato A
  item: Kuno M
  item: Seki N
  item: Sakane K

Adenosine deaminase converts purine riboside into an analogue of a reactive intermediate: a 13C NMR and kinetic study.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3442668
journal: Biochemistry
volume: 26
pages: 8450-7
published year: 1987
authors:
  item: Kurz LC
  item: Frieden C

Evidence from nitrogen-15 and solvent deuterium isotope effects on the chemical mechanism of adenosine deaminase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3427079
journal: Biochemistry
volume: 26
pages: 7378-84
published year: 1987
authors:
  item: Weiss PM
  item: Cook PF
  item: Hermes JD
  item: Cleland WW

Preliminary X-ray analysis of crystals of murine adenosine deaminase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3398052
journal: J Mol Biol
volume: 200
pages: 613-4
published year: 1988
authors:
  item: Wilson DK
  item: Rudolph FB
  item: Harrison ML
  item: Kellems RE
  item: Quiocho FA

http://ezcatdb.cbrc.jp/EzCatDB/reference/S00232#4
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2713361
journal: Biochemistry
volume: 28
pages: 1242-7
published year: 1989
authors:
  item: Jones W
  item: Kurz LC
  item: Wolfenden R
title: Transition-state stabilization by adenosine deaminase: 1,6-addition of water to purine ribonucleoside, the enzyme's affinity for 6-hydroxy-1,6-dihydropurine ribonucleoside, and the effective concentration of substrate water at the active site.

Structural and conformational analysis of pentostatin (2'-deoxycoformycin), a potent inhibitor of adenosine deaminase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2275794
journal: J Biomol Struct Dyn
volume: 8
pages: 199-212
published year: 1990
authors:
  item: Cox MB
  item: Arjunan P
  item: Arora SK

Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
medline id: 92022516
references: http://www.ncbi.nlm.nih.gov/pubmed/1925539
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P03958
journal: Science
volume: 252
pages: 1278-84
published year: 1991
authors:
  item: Wilson DK
  item: Rudolph FB
  item: Quiocho FA

A transition state in pieces: major contributions of entropic effects to ligand binding by adenosine deaminase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1510925
journal: Biochemistry
volume: 31
pages: 7356-66
published year: 1992
authors:
  item: Kati WM
  item: Acheson SA
  item: Wolfenden R

The rate of formation of transition-state analogues in the active site of adenosine deaminase is encounter-controlled: implications for the mechanism.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1731884
journal: Biochemistry
volume: 31
pages: 39-48
published year: 1992
authors:
  item: Kurz LC
  item: Moix L
  item: Riley MC
  item: Frieden C

Refined 2.5 A structure of murine adenosine deaminase at pH 6.0.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1518061
journal: J Mol Biol
volume: 226
pages: 917-21
published year: 1992
authors:
  item: Sharff AJ
  item: Wilson DK
  item: Chang Z
  item: Quiocho FA

A pre-transition-state mimic of an enzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/8439534
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biochemistry
volume: 32
pages: 1689-94
published year: 1993
authors:
  item: Wilson DK
  item: Quiocho FA

Site-directed mutagenesis of active site glutamate-217 in mouse adenosine deaminase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8634299
journal: Biochemistry
volume: 35
pages: 1672-80
published year: 1996
authors:
  item: Mohamedali KA
  item: Kurz LC
  item: Rudolph FB

Probing the functional role of two conserved active site aspartates in mouse adenosine deaminase.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/8672487
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biochemistry
volume: 35
pages: 7862-72
published year: 1996
authors:
  item: Sideraki V
  item: Mohamedali KA
  item: Wilson DK
  item: Chang Z
  item: Kellems RE
  item: Quiocho FA
  item: Rudolph FB

An adenosine deaminase (ADA) allele contains two newly identified deleterious mutations (Y97C and L106V) that interact to abolish enzyme activity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9361033
journal: Hum Mol Genet
volume: 6
pages: 2271-8
published year: 1997
authors:
  item: Jiang C
  item: Hong R
  item: Horowitz SD
  item: Kong X
  item: Hirschhorn R

http://ezcatdb.cbrc.jp/EzCatDB/reference/S00232#18
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9341908
journal: J Med Chem
volume: 40
pages: 3336-45
published year: 1997
authors:
  item: Groziak MP
  item: Huan ZW
  item: Ding H
  item: Meng Z
  item: Stevens WC
  item: Robinson PD
title: Effect of a chemical modification on the hydrated adenosine intermediate produced by adenosine deaminase and a model reaction for a potential mechanism of action of 5-aminoimidazole ribonucleotide carboxylase.

Characterization of hydrogen bonding in the complex of adenosine deaminase with a transition state analogue: a Raman spectroscopic study.
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references: http://www.ncbi.nlm.nih.gov/pubmed/9538015
journal: Biochemistry
volume: 37
pages: 4968-76
published year: 1998
authors:
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  item: Rudolph FB
  item: Callender R

Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH of maximum activity.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
medline id: 98285559
references: http://www.ncbi.nlm.nih.gov/pubmed/9622483
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P03958
journal: Biochemistry
volume: 37
pages: 8314-24
published year: 1998
authors:
  item: Wang Z
  item: Quiocho FA

Probing the active site of adenosine deaminase by a pH responsive fluorescent competitive inhibitor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9474762
journal: Biophys Chem
volume: 70
pages: 41-56
published year: 1998
authors:
  item: Caiolfa VR
  item: Gill D
  item: Parola AH

Adenosine deaminase prefers a distinct sugar ring conformation for binding and catalysis: kinetic and structural studies.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10704207
journal: Biochemistry
volume: 39
pages: 2581-92
published year: 2000
authors:
  item: Ford H Jr
  item: Dai F
  item: Mu L
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  item: Nicklaus MC
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  item: Barchi JJ Jr

3'-Beta-ethynyl and 2'-deoxy-3'-beta-ethynyl adenosines: first 3'-beta-branched-adenosines substrates of adenosine deaminase.
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references: http://www.ncbi.nlm.nih.gov/pubmed/10673097
journal: Bioorg Med Chem Lett
volume: 10
pages: 139-41
published year: 2000
authors:
  item: Tritsch D
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  item: Burger A
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http://ezcatdb.cbrc.jp/EzCatDB/reference/S00232#24
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12057661
journal: Bioorg Med Chem
volume: 10
pages: 2723-30
published year: 2002
authors:
  item: Hernandez S
  item: Ford H Jr
  item: Marquez VE
title: Is the anomeric effect an important factor in the rate of adenosine deaminase catalyzed hydrolysis of purine nucleosides? A direct comparison of nucleoside analogues constructed on ribose and carbocyclic templates with equivalent heterocyclic bases selected to promote hydration.

Clustered charged amino acids of human adenosine deaminase comprise a functional epitope for binding the adenosine deaminase complexing protein CD26/dipeptidyl peptidase IV.
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references: http://www.ncbi.nlm.nih.gov/pubmed/11901152
journal: J Biol Chem
volume: 277
pages: 19720-6
published year: 2002
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The stability curve of bovine adenosine deaminase is bimodal.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12437375
journal: J Biomol Struct Dyn
volume: 20
pages: 375-80
published year: 2002
authors:
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  item: Britt BM

Structure of bovine adenosine deaminase complexed with 6-hydroxy-1,6-dihydropurine riboside.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/12554940
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journal: Acta Crystallogr D Biol Crystallogr
volume: 59
pages: 299-303
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  item: Fujii T

A highly potent non-nucleoside adenosine deaminase inhibitor: efficient drug discovery by intentional lead hybridization.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/14709046
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journal: J Am Chem Soc
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Crystal structure of CD26/dipeptidyl-peptidase IV in complex with adenosine deaminase reveals a highly amphiphilic interface.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/15213224
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Structure-based design, synthesis, and structure-activity relationship studies of novel non-nucleoside adenosine deaminase inhibitors.
type: BibliographicResource
comment: X-ray crystallography
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Structure-based design and synthesis of non-nucleoside, potent, and orally bioavailable adenosine deaminase inhibitors.
type: BibliographicResource
comment: X-ray crystallography
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journal: J Med Chem
volume: 47
pages: 2728-31
published year: 2004
authors:
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  item: Kato Y
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Crystal structures of HIV-1 Tat derived nonapeptides Tat(1-9) and Trp2-Tat(1-9) bound to the active site of dipeptidyl peptidase IV (CD26).
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/15695814
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Biol Chem
volume: [Epub ahead of print]
pages: [Epub ahead of print]
published year: 2005
authors:
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  item: Liu J
  item: Reutter W
  item: Saenger W
  item: Fan H

deoxyadenosine deaminase
type: KeggEnzyme

Analogue
compound: Adenosine
pdb: 1addA
ligand het code: 1DA

Analogue
compound: Adenosine
pdb: 1fkwA
ligand het code: PUR

Analogue
compound: Adenosine
pdb: 1uipA
ligand het code: PUR

IntermediateAnalogue
compound: 6-Hydroxy-adenosine
pdb: 1a4lA
ligand het code: DCF

IntermediateAnalogue
compound: 6-Hydroxy-adenosine
pdb: 1a4lB
ligand het code: DCF

IntermediateAnalogue
compound: 6-Hydroxy-adenosine
pdb: 1a4lC
ligand het code: DCF

IntermediateAnalogue
compound: 6-Hydroxy-adenosine
pdb: 1a4lD
ligand het code: DCF

IntermediateAnalogue
compound: 6-Hydroxy-adenosine
pdb: 1a4mA
ligand het code: PRH

IntermediateAnalogue
compound: 6-Hydroxy-adenosine
pdb: 1a4mB
ligand het code: PRH

IntermediateAnalogue
compound: 6-Hydroxy-adenosine
pdb: 1a4mC
ligand het code: PRH

IntermediateAnalogue
compound: 6-Hydroxy-adenosine
pdb: 1a4mD
ligand het code: PRH

IntermediateAnalogue
compound: 6-Hydroxy-adenosine
pdb: 1fkxA
ligand het code: PRH

IntermediateAnalogue
compound: 6-Hydroxy-adenosine
pdb: 1uioA
ligand het code: HPR

IntermediateAnalogue
compound: 6-Hydroxy-adenosine
pdb: 2adaA
ligand het code: HPR

IntermediateAnalogue
compound: 6-Hydroxy-adenosine
pdb: 1krmA
ligand het code: PRH

ReferenceForCatalyticMechanism
reference index: 1
reference section: p.8455-8456

ReferenceForCatalyticMechanism
reference index: 2
reference section: p.7382-7383

ReferenceForCatalyticMechanism
reference index: 4
reference section: p.1246-1247

ReferenceForCatalyticMechanism
reference index: 6
reference section: Fig.4, p.1282-1283

ReferenceForCatalyticMechanism
reference index: 7
reference section: p.7364-7365

ReferenceForCatalyticMechanism
reference index: 10
reference section: Fig.3, p.1692-1693

ReferenceForCatalyticMechanism
reference index: 11
reference section: p.693

ReferenceForCatalyticMechanism
reference index: 12

ReferenceForCatalyticMechanism
reference index: 13
reference section: Scheme 1

ReferenceForCatalyticMechanism
reference index: 14
reference section: Fig.1, p.7863, p.7871

ReferenceForCatalyticMechanism
reference index: 15
reference section: Fig.1, p.15027-15028

ReferenceForCatalyticMechanism
reference index: 19
reference section: p.4974-4975

ReferenceForCatalyticMechanism
reference index: 20
reference section: p.8322-8323

ReferenceForCatalyticMechanism
reference index: 22
reference section: p.2589-2590