aldehyde dehydrogenase (pyrroloquinoline-quinone)

Identifiers
EC no.| 1.2.99.3
CAS no.| 75536-77-5
Databases
IntEnz| IntEnz view
BRENDA| BRENDA entry
ExPASy| NiceZyme view
KEGG| KEGG entry
MetaCyc| metabolic pathway
PRIAM| profile
PDB structures| RCSB PDB PDBe PDBsum
Gene Ontology| AmiGO  / QuickGO
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PMC| articles
PubMed| articles
NCBI| proteins

In enzymology, an aldehyde dehydrogenase (pyrroloquinoline-quinone) (EC 1.2.99.3) is an enzyme that catalyzes the chemical reaction

an aldehyde + acceptor + H2O  ⇌ {\displaystyle \rightleftharpoons } a carboxylate + reduced acceptor

The 3 substrates of this enzyme are aldehyde, acceptor, and H2O, whereas its two products are carboxylate and reduced acceptor.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is aldehyde:(pyrroloquinoline-quinone) oxidoreductase. This enzyme is also called aldehyde dehydrogenase (acceptor). This enzyme participates in 4 metabolic pathways: fatty acid metabolism, pyruvate metabolism, propanoate metabolism, and butanoate metabolism. It employs one cofactor, PQQ.

## References

[edit]

* Ameyama M; Adachi O (1982). "Aldehyde dehydrogenase from acetic acid bacteria, membrane-bound". Carbohydrate Metabolism - Part D. Methods Enzymol. Vol. 89\. pp. 491–497\. doi:10.1016/S0076-6879(82)89084-8. ISBN 978-0-12-181989-7.491-497&rft.date=1982&rft_id=info:doi/10.1016/S0076-6879(82)89084-8&rft.isbn=978-0-12-181989-7&rft.au=Ameyama+M&rft.au=Adachi+O&rfr_id=info:sid/en.wikipedia.org:Aldehyde+dehydrogenase+(pyrroloquinoline-quinone)" class="Z3988">
* Ameyama M, Osada K, Shinagawa E, Matsushita K, Adachi O (1981). "Purification and characterization of aldehyde dehydrogenase of Acetobacter aceti". Agric. Biol. Chem. 45 (8): 1889–1890\. doi:10.1271/bbb1961.45.1889.1889-1890&rft.date=1981&rft_id=info:doi/10.1271/bbb1961.45.1889&rft.aulast=Ameyama&rft.aufirst=M&rft.au=Osada,+K&rft.au=Shinagawa,+E&rft.au=Matsushita,+K&rft.au=Adachi,+O&rft_id=https://doi.org/10.1271%2Fbbb1961.45.1889&rfr_id=info:sid/en.wikipedia.org:Aldehyde+dehydrogenase+(pyrroloquinoline-quinone)" class="Z3988">
* Patel RN, Hou CT, Derelanko P, Felix A (1980). "Purification and properties of a heme-containing aldehyde dehydrogenase from Methylosinus trichosporium". Arch. Biochem. Biophys. 203 (2): 654–62\. doi:10.1016/0003-9861(80)90223-4. PMID 6779711.654-62&rft.date=1980&rft_id=info:doi/10.1016/0003-9861(80)90223-4&rft_id=info:pmid/6779711&rft.aulast=Patel&rft.aufirst=RN&rft.au=Hou,+CT&rft.au=Derelanko,+P&rft.au=Felix,+A&rfr_id=info:sid/en.wikipedia.org:Aldehyde+dehydrogenase+(pyrroloquinoline-quinone)" class="Z3988">

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Aldehyde/oxo oxidoreductases (EC 1.2)

1.2.1: NAD or NADP|

* Aldehyde dehydrogenase
* Acetaldehyde dehydrogenase
* Long-chain-aldehyde dehydrogenase
* Mycothiol-dependent formaldehyde dehydrogenase

1.2.2: cytochrome|

* Formate dehydrogenase (cytochrome)

1.2.3: oxygen|

* Aldehyde oxidase

1.2.4: disulfide|

* Oxoglutarate dehydrogenase complex
* Pyruvate dehydrogenase
* Branched-chain alpha-keto acid dehydrogenase complex
* BCKDHA
* BCKDHB
* DBT
* DLD

1.2.7: iron–sulfur protein|

* Pyruvate synthase

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Enzymes

Activity|

* Active site
* Binding site
* Catalytic triad
* Oxyanion hole
* Enzyme promiscuity
* Diffusion-limited enzyme
* Cofactor
* Enzyme catalysis

Regulation|

* Allosteric regulation
* Cooperativity
* Enzyme inhibitor
* Enzyme activator

Classification|

* EC number
* Enzyme superfamily
* Enzyme family
* List of enzymes

Kinetics|

* Enzyme kinetics
* Eadie–Hofstee diagram
* Hanes–Woolf plot
* Lineweaver–Burk plot
* Michaelis–Menten kinetics

Types|

* EC1 Oxidoreductases (list)
* EC2 Transferases (list)
* EC3 Hydrolases (list)
* EC4 Lyases (list)
* EC5 Isomerases (list)
* EC6 Ligases (list)
* EC7 Translocases (list)

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