PDBsum entry: 1eyy

Oxidoreductase

PDB id: 1eyy

Contents

Protein chains

504 a.a. *

Ligands

NAP ×4

Waters ×413

* Residue conservation analysis

PDB id:

1eyy

Name:

Oxidoreductase

Title:

Crystal structure of the NADP+ dependent aldehyde dehydrogen vibrio harveyi.

Structure:

Aldehyde dehydrogenase. Chain: a, b, c, d. Synonym: aldh. Engineered: yes

Source:

Vibrio harveyi. Organism_taxid: 669. Strain: b392. Gene: aldh. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

2.50Å R-factor: 0.206 R-free: 0.239

Authors:

B.Ahvazi,R.Coulombe,M.Delarge,M.Vedadi,L.Zhang,E.Meighen,A.V

Key ref:

B.Ahvazi et al. (2000). Crystal structure of the NADP+-dependent aldehyde dehydrogenase from Vibrio harveyi: structural implications for cofactor specificity and affinity. Biochem J, 349, 853-861. PubMed id: 10903148 Ref: Full text

Date:

09-May-00 Release date: 24-May-00

Supersedes:

1cbz

Protein chains

Q56694  (ALDH_VIBHA) -  NADP-dependent fatty aldehyde dehydrogenase

Seq: 510 a.a.

Struc: 504 a.a.

Enzyme reactions

• Enzyme class: E.C.1.2.1.4 - Aldehyde dehydrogenase (NADP(+)).
• Reaction: An aldehyde + NADP⁺ + H₂O = a carboxylate + NADPH

aldehyde + NADP(+) (Bound ligand (Het Group name = NAP) matches with 64.58% similarity) + H(2)O = carboxylate + NADPH

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Biological process: metabolic process (2 terms)
• Biochemical function: oxidoreductase activity (3 terms)

reference

Full text	Biochem J 349:853-861 (2000)
PubMed id: 10903148

Crystal structure of the NADP+-dependent aldehyde dehydrogenase from Vibrio harveyi: structural implications for cofactor specificity and affinity.

B.Ahvazi, R.Coulombe, M.Delarge, M.Vedadi, L.Zhang, E.Meighen, A.Vrielink.

ABSTRACT

Aldehyde dehydrogenase from the bioluminescent bacterium, Vibrio harveyi, catalyses the oxidation of long-chain aliphatic aldehydes to acids. The enzyme is unique compared with other forms of aldehyde dehydrogenase in that it exhibits a very high specificity and affinity for the cofactor NADP(+). Structural studies of this enzyme and comparisons with other forms of aldehyde dehydrogenase provide the basis for understanding the molecular features that dictate these unique properties and will enhance our understanding of the mechanism of catalysis for this class of enzyme. The X-ray structure of aldehyde dehydrogenase from V. harveyi has been solved to 2.5-A resolution as a partial complex with the cofactor NADP(+) and to 2. 1-A resolution as a fully bound 'holo' complex. The cofactor preference exhibited by different forms of the enzyme is predominantly determined by the electrostatic environment surrounding the 2'-hydroxy or the 2'-phosphate groups of the adenosine ribose moiety of NAD(+) or NADP(+), respectively. In the NADP(+)-dependent structures the presence of a threonine and a lysine contribute to the cofactor specificity. In the V. harveyi enzyme an arginine residue (Arg-210) contributes to the high cofactor affinity through a pi stacking interaction with the adenine ring system of the cofactor. Further differences between the V. harveyi enzyme and other aldehyde dehydrogenases are seen in the active site, in particular a histidine residue which is structurally conserved with phosphorylating glyceraldehyde-3-phosphate dehydrogenase. This may suggest an alternative mechanism for activation of the reactive cysteine residue for nucleophilic attack.