PDBsum entry 6tqh

Oxidoreductase

PDB id: 6tqh

Contents

Protein chains

869 a.a.

419 a.a.

Ligands

NAD ×4

Metals

_FE ×2

PDB id:

6tqh

Name:

Oxidoreductase

Title:

Escherichia coli adhe structure in its extended conformation

Structure:

Aldehyde-alcohol dehydrogenase. Chain: a, f, c, b. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Gene: adhe, ana, b1241, jw1228. Expressed in: escherichia coli. Expression_system_taxid: 562

Authors:

R.Fronzes,P.Pony

Key ref:

P.Pony et al. (2020). Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation. Nat Commun, 11, 1426. PubMed id: 32188856 DOI: 10.1038/s41467-020-15214-y

Date:

16-Dec-19 Release date: 03-Jun-20

Protein chains

P0A9Q7  (ADHE_ECOLI) -  Bifunctional aldehyde-alcohol dehydrogenase AdhE from Escherichia coli (strain K12)

Seq: 891 a.a.

Struc: 869 a.a.

Protein chains

P0A9Q7  (ADHE_ECOLI) -  Bifunctional aldehyde-alcohol dehydrogenase AdhE from Escherichia coli (strain K12)

Seq: 891 a.a.

Struc: 419 a.a.

Enzyme reactions

• Enzyme class 1: Chains A, F, C, B: E.C.1.1.1.1 - alcohol dehydrogenase.
• Reaction:
  1. a primary alcohol + NAD⁺ = an aldehyde + NADH + H⁺
  2. a secondary alcohol + NAD⁺ = a ketone + NADH + H⁺

primary alcohol + NAD(+) (Bound ligand (Het Group name = NAD) corresponds exactly) = aldehyde + NADH + H(+)

secondary alcohol + NAD(+) (Bound ligand (Het Group name = NAD) corresponds exactly) = ketone + NADH + H(+)

• Cofactor: Zn(2+) or Fe cation
• Enzyme class 2: Chains A, F, C, B: E.C.1.2.1.10 - acetaldehyde dehydrogenase (acetylating).
• Reaction: acetaldehyde + NAD⁺ + CoA = acetyl-CoA + NADH + H⁺

acetaldehyde + NAD(+) (Bound ligand (Het Group name = NAD) corresponds exactly) + CoA = acetyl-CoA + NADH + H(+)

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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

reference

DOI no: 10.1038/s41467-020-15214-y

Nat Commun 11:1426 (2020)

PubMed id: 32188856

Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation.

P.Pony, C.Rapisarda, L.Terradot, E.Marza, R.Fronzes.

ABSTRACT

Acetaldehyde-alcohol dehydrogenase (AdhE) enzymes are a key metabolic enzyme in bacterial physiology and pathogenicity. They convert acetyl-CoA to ethanol via an acetaldehyde intermediate during ethanol fermentation in an anaerobic environment. This two-step reaction is associated to NAD⁺ regeneration, essential for glycolysis. The bifunctional AdhE enzyme is conserved in all bacterial kingdoms but also in more phylogenetically distant microorganisms such as green microalgae. It is found as an oligomeric form called spirosomes, for which the function remains elusive. Here, we use cryo-electron microscopy to obtain structures of Escherichia coli spirosomes in different conformational states. We show that spirosomes contain active AdhE monomers, and that AdhE filamentation is essential for its activity in vitro and function in vivo. The detailed analysis of these structures provides insight showing that AdhE filamentation is essential for substrate channeling within the filament and for the regulation of enzyme activity.