DB code: D00020

CATH domain 3.40.605.10 : Aldehyde Dehydrogenase; Chain A, domain 1 Catalytic domain
3.40.309.10 : Aldehyde Dehydrogenase; Chain A, domain 2 Catalytic domain
E.C. 1.2.1.5
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.309.10 : Aldehyde Dehydrogenase; Chain A, domain 2 D00021 D00022 D00475 D00614
3.40.605.10 : Aldehyde Dehydrogenase; Chain A, domain 1 D00021 D00022 D00475 D00614

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P11883 Aldehyde dehydrogenase, dimeric NADP-preferring
EC 1.2.1.5
Aldehyde dehydrogenase family 3 member A1
Tumor-associated aldehyde dehydrogenase
HTC-ALDH
NP_114178.1 (Protein)
NM_031972.1 (DNA/RNA sequence)
PF00171 (Aldedh)
[Graphical View]

KEGG enzyme name
aldehyde dehydrogenase [NAD(P)+]
aldehyde dehydrogenase [NAD(P)+]
ALDH

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P11883 AL3A1_RAT An aldehyde + NAD(P)(+) + H(2)O = an acid + NAD(P)H. Homodimer. Cytoplasm.

KEGG Pathways
Map code Pathways E.C.
MAP00010 Glycolysis / Gluconeogenesis
MAP00340 Histidine metabolism
MAP00350 Tyrosine metabolism
MAP00360 Phenylalanine metabolism
MAP00980 Metabolism of xenobiotics by cytochrome P450
MAP00982 Drug metabolism - cytochrome P450

Compound table
Substrates Products Intermediates
KEGG-id C00071 C00006 C00003 C00001 C00174 C00005 C00004 C00080
E.C.
Compound Aldehyde NADP+ NAD+ H2O Acid NADPH NADH H+
Type carbohydrate amide group,amine group,nucleotide amide group,amine group,nucleotide H2O others amide group,amine group,nucleotide amide group,amine group,nucleotide others
ChEBI 18009
 18009
 		15846
 15846
 		15377
 15377
 		16474
 16474
 		16908
 16908
 		15378
 15378
PubChem 5886
 5886
 		5893
 5893
 		22247451
 962
 22247451
 962
 		5884
 5884
 		439153
 439153
 		1038
 1038
1ad3A01 Unbound Unbound Bound:NAD Unbound Unbound Unbound
1ad3B01 Unbound Unbound Bound:NAD Unbound Unbound Unbound
1ad3A02 Unbound Unbound Unbound Unbound Unbound Unbound
1ad3B02 Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1ad3 & Swiss-prot;P11883 & literature [6], [7]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ad3A01 ASN 114
1ad3B01 ASN 114
1ad3A02 CYS 243;GLU 333
1ad3B02 CYS 243;GLU 333

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[6]
Fig.7a, p.324
[7]
Fig.2, p.55-58
[9]
[14]

References
[1]
Resource
Comments
Medline ID
PubMed ID 2713359
Journal Biochemistry
Year 1989
Volume 28
Pages 1160-7
Authors Hempel J, Harper K, Lindahl R
Title Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID 91219392
PubMed ID 2091023
Journal Proteins
Year 1990
Volume 8
Pages 305-8
Authors Rose JP, Hempel J, Kuo I, Lindahl R, Wang BC
Title Preliminary crystallographic analysis of class 3 rat liver aldehyde dehydrogenase.
Related PDB
Related UniProtKB P11883
[3]
Resource
Comments
Medline ID
PubMed ID 7484412
Journal Adv Exp Med Biol
Year 1995
Volume 372
Pages 71-7
Authors Sun J, Hempel J, Lindahl R, Perozich J, Rose J, Wang BC
Title Progress toward the tertiary structure of (class 3) aldehyde dehydrogenase.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 9059601
Journal Adv Exp Med Biol
Year 1997
Volume 414
Pages 9-13
Authors Hempel J, Liu ZJ, Perozich J, Rose J, Lindahl R, Wang BC
Title Conserved residues in the aldehyde dehydrogenase family. Locations in the class 3 tertiary structure.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 9059600
Journal Adv Exp Med Biol
Year 1997
Volume 414
Pages 1-7
Authors Liu ZJ, Hempel J, Sun J, Rose J, Hsiao D, Chang WR, Chung YJ, Kuo I, Lindahl R, Wang BC
Title Crystal structure of a class 3 aldehyde dehydrogenase at 2.6 A resolution.
Related PDB
Related UniProtKB
[6]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)
Medline ID 97249296
PubMed ID 9095201
Journal Nat Struct Biol
Year 1997
Volume 4
Pages 317-26
Authors Liu ZJ, Sun YJ, Rose J, Chung YJ, Hsiao CD, Chang WR, Kuo I, Perozich J, Lindahl R, Hempel J, Wang BC
Title The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold.
Related PDB 1ad3
Related UniProtKB P11883
[7]
Resource
Comments
Medline ID
PubMed ID 10352669
Journal Adv Exp Med Biol
Year 1999
Volume 463
Pages 53-9
Authors Hempel J, Perozich J, Chapman T, Rose J, Boesch JS, Liu ZJ, Lindahl R, Wang BC
Title Aldehyde dehydrogenase catalytic mechanism. A proposal.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 11012673
Journal Eur J Biochem
Year 2000
Volume 267
Pages 6197-203
Authors Perozich J, Kuo I, Wang BC, Boesch JS, Lindahl R, Hempel J
Title Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 11306029
Journal Chem Biol Interact
Year 2001
Volume 130-132
Pages 39-46
Authors Hempel J, Lindahl R, Perozich J, Wang B, Kuo I, Nicholas H
Title Beyond the catalytic core of ALDH: a web of important residues begins to emerge.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 11306036
Journal Chem Biol Interact
Year 2001
Volume 130-132
Pages 115-24
Authors Perozich J, Kuo I, Lindahl R, Hempel J
Title Coenzyme specificity in aldehyde dehydrogenase.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11306039
Journal Chem Biol Interact
Year 2001
Volume 130-132
Pages 151-60
Authors Rodriguez-Zavala J, Weiner H
Title Role of the C-terminal tail on the quaternary structure of aldehyde dehydrogenases.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 11306041
Journal Chem Biol Interact
Year 2001
Volume 130-132
Pages 173-9
Authors Wei B, Weiner H
Title Making an Oriental equivalent of the yeast cytosolic aldehyde dehydrogenase as well as making one with positive cooperativity in coenzyme binding by mutations of glutamate 492 and arginine 480.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 11306044
Journal Chem Biol Interact
Year 2001
Volume 130-132
Pages 201-7
Authors Wymore T, Nicholas HB, Hempel J
Title Molecular dynamics simulation of class 3 aldehyde dehydrogenase.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 11168411
Journal Eur J Biochem
Year 2001
Volume 268
Pages 722-6
Authors Hempel J, Kuo I, Perozich J, Wang BC, Lindahl R, Nicholas H
Title Aldehyde dehydrogenase. Maintaining critical active site geometry at motif 8 in the class 3 enzyme.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 11790142
Journal J Biomol Struct Dyn
Year 2001
Volume 19
Pages 429-47
Authors Izaguirre G, Pietruszko R, Cho S, MacKerell A Jr
Title Human aldehyde dehydrogenase catalytic activity and structural interactions with coenzyme analogs.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 12081471
Journal Biochemistry
Year 2002
Volume 41
Pages 8229-37
Authors Rodriguez-Zavala JS, Weiner H
Title Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to aldehyde dehydrogenase superfamily. This enzyme belongs to the class-3 of the superfamily.

Created Updated
2004-03-24 2009-02-26