EzCatDB: D00020
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DB codeD00020
CATH domainDomain 13.40.605.10 : Aldehyde Dehydrogenase; Chain A, domain 1Catalytic domain
Domain 23.40.309.10 : Aldehyde Dehydrogenase; Chain A, domain 2Catalytic domain
E.C.1.2.1.5

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

Enzyme Name
UniProtKBKEGG

P11883
Protein nameAldehyde dehydrogenase, dimeric NADP-preferringaldehyde dehydrogenase [NAD(P)+]
aldehyde dehydrogenase [NAD(P)+]
ALDH
SynonymsEC 1.2.1.5
Aldehyde dehydrogenase family 3 member A1
Tumor-associated aldehyde dehydrogenase
HTC-ALDH
RefSeqNP_114178.1 (Protein)
NM_031972.1 (DNA/RNA sequence)
PfamPF00171 (Aldedh)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00010Glycolysis / Gluconeogenesis
MAP00340Histidine metabolism
MAP00350Tyrosine metabolism
MAP00360Phenylalanine metabolism
MAP00980Metabolism of xenobiotics by cytochrome P450
MAP00982Drug metabolism - cytochrome P450

UniProtKB:Accession NumberP11883
Entry nameAL3A1_RAT
ActivityAn aldehyde + NAD(P)(+) + H(2)O = an acid + NAD(P)H.
SubunitHomodimer.
Subcellular locationCytoplasm.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00071C00006C00003C00001C00174C00005C00004C00080
CompoundAldehydeNADP+NAD+H2OAcidNADPHNADHH+
Typecarbohydrateamide group,amine group,nucleotideamide group,amine group,nucleotideH2Oothersamide group,amine group,nucleotideamide group,amine group,nucleotideothers
ChEBI
18009
15846
15377

16474
16908
15378
PubChem
5886
5893
962
22247451

5884
439153
1038
                
1ad3A01UnboundUnboundBound:NAD UnboundUnboundUnbound 
1ad3B01UnboundUnboundBound:NAD UnboundUnboundUnbound 
1ad3A02UnboundUnboundUnbound UnboundUnboundUnbound 
1ad3B02UnboundUnboundUnbound UnboundUnboundUnbound 

Active-site residues
resource
PDB;1ad3 & Swiss-prot;P11883 & literature [6], [7]
pdbCatalytic residues
         
1ad3A01ASN 114
1ad3B01ASN 114
1ad3A02CYS 243;GLU 333
1ad3B02CYS 243;GLU 333

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[6]Fig.7a, p.324
[7]Fig.2, p.55-58
[9]

[14]


references
[1]
PubMed ID2713359
JournalBiochemistry
Year1989
Volume28
Pages1160-7
AuthorsHempel J, Harper K, Lindahl R
TitleInducible (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.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID91219392
PubMed ID2091023
JournalProteins
Year1990
Volume8
Pages305-8
AuthorsRose JP, Hempel J, Kuo I, Lindahl R, Wang BC
TitlePreliminary crystallographic analysis of class 3 rat liver aldehyde dehydrogenase.
Related UniProtKBP11883
[3]
PubMed ID7484412
JournalAdv Exp Med Biol
Year1995
Volume372
Pages71-7
AuthorsSun J, Hempel J, Lindahl R, Perozich J, Rose J, Wang BC
TitleProgress toward the tertiary structure of (class 3) aldehyde dehydrogenase.
[4]
PubMed ID9059601
JournalAdv Exp Med Biol
Year1997
Volume414
Pages9-13
AuthorsHempel J, Liu ZJ, Perozich J, Rose J, Lindahl R, Wang BC
TitleConserved residues in the aldehyde dehydrogenase family. Locations in the class 3 tertiary structure.
[5]
PubMed ID9059600
JournalAdv Exp Med Biol
Year1997
Volume414
Pages1-7
AuthorsLiu ZJ, Hempel J, Sun J, Rose J, Hsiao D, Chang WR, Chung YJ, Kuo I, Lindahl R, Wang BC
TitleCrystal structure of a class 3 aldehyde dehydrogenase at 2.6 A resolution.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)
Medline ID97249296
PubMed ID9095201
JournalNat Struct Biol
Year1997
Volume4
Pages317-26
AuthorsLiu ZJ, Sun YJ, Rose J, Chung YJ, Hsiao CD, Chang WR, Kuo I, Perozich J, Lindahl R, Hempel J, Wang BC
TitleThe first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold.
Related PDB1ad3
Related UniProtKBP11883
[7]
PubMed ID10352669
JournalAdv Exp Med Biol
Year1999
Volume463
Pages53-9
AuthorsHempel J, Perozich J, Chapman T, Rose J, Boesch JS, Liu ZJ, Lindahl R, Wang BC
TitleAldehyde dehydrogenase catalytic mechanism. A proposal.
[8]
PubMed ID11012673
JournalEur J Biochem
Year2000
Volume267
Pages6197-203
AuthorsPerozich J, Kuo I, Wang BC, Boesch JS, Lindahl R, Hempel J
TitleShifting the NAD/NADP preference in class 3 aldehyde dehydrogenase.
[9]
PubMed ID11306029
JournalChem Biol Interact
Year2001
Volume130-132
Pages39-46
AuthorsHempel J, Lindahl R, Perozich J, Wang B, Kuo I, Nicholas H
TitleBeyond the catalytic core of ALDH: a web of important residues begins to emerge.
[10]
PubMed ID11306036
JournalChem Biol Interact
Year2001
Volume130-132
Pages115-24
AuthorsPerozich J, Kuo I, Lindahl R, Hempel J
TitleCoenzyme specificity in aldehyde dehydrogenase.
[11]
PubMed ID11306039
JournalChem Biol Interact
Year2001
Volume130-132
Pages151-60
AuthorsRodriguez-Zavala J, Weiner H
TitleRole of the C-terminal tail on the quaternary structure of aldehyde dehydrogenases.
[12]
PubMed ID11306041
JournalChem Biol Interact
Year2001
Volume130-132
Pages173-9
AuthorsWei B, Weiner H
TitleMaking 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.
[13]
PubMed ID11306044
JournalChem Biol Interact
Year2001
Volume130-132
Pages201-7
AuthorsWymore T, Nicholas HB, Hempel J
TitleMolecular dynamics simulation of class 3 aldehyde dehydrogenase.
[14]
PubMed ID11168411
JournalEur J Biochem
Year2001
Volume268
Pages722-6
AuthorsHempel J, Kuo I, Perozich J, Wang BC, Lindahl R, Nicholas H
TitleAldehyde dehydrogenase. Maintaining critical active site geometry at motif 8 in the class 3 enzyme.
[15]
PubMed ID11790142
JournalJ Biomol Struct Dyn
Year2001
Volume19
Pages429-47
AuthorsIzaguirre G, Pietruszko R, Cho S, MacKerell A Jr
TitleHuman aldehyde dehydrogenase catalytic activity and structural interactions with coenzyme analogs.
[16]
PubMed ID12081471
JournalBiochemistry
Year2002
Volume41
Pages8229-37
AuthorsRodriguez-Zavala JS, Weiner H
TitleStructural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation.

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

createdupdated
2004-03-242009-02-26


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