Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

MetaCyc Reaction: 1.1.9.1

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Protein-Modification Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions Protein-Modification Reactions

EC Number: 1.1.9.1

Enzymes and Genes:
alcohol dehydrogenase (azurin) Inferred from experiment : qheDH ( Comamonas testosteroni )

Supersedes EC number: 1.1.98.1

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Undetermined; a substrate lacks a chemical formula

Enzyme Commission Primary Name: alcohol dehydrogenase (azurin)

Enzyme Commission Synonyms: type II quinoprotein alcohol dehydrogenase, quinohaemoprotein ethanol dehydrogenase, QHEDH, ADHIIB

Enzyme Commission Summary:
A soluble, periplasmic PQQ-containing quinohaemoprotein. Also contains a single haem c. Occurs in Comamonas and Pseudomonas. Does not require an amine activator. Oxidises a wide range of primary and secondary alcohols, and also aldehydes and large substrates such as sterols; methanol is not a substrate. Usually assayed with phenazine methosulphate or ferricyanide. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulphide ring structure in close proximity to the PQQ.

Citations: [Groen86, deJong95, Toyama95, Matsushita99, Chen02, Oubrie02]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:1.1.9.1 , ENZYME:EC:1.1.9.1 , IUBMB-ExplorEnz:EC:1.1.9.1

Credits:
Created 17-Mar-2010 by Caspi R , SRI International


References

Chen02: Chen ZW, Matsushita K, Yamashita T, Fujii TA, Toyama H, Adachi O, Bellamy HD, Mathews FS (2002). "Structure at 1.9 A resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5." Structure 10(6);837-49. PMID: 12057198

deJong95: de Jong GA, Caldeira J, Sun J, Jongejan JA, de Vries S, Loehr TM, Moura I, Moura JJ, Duine JA (1995). "Characterization of the interaction between PQQ and heme c in the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni." Biochemistry 34(29);9451-8. PMID: 7626615

Groen86: Groen BW, van Kleef MA, Duine JA (1986). "Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni." Biochem J 234(3);611-5. PMID: 3521592

Matsushita99: Matsushita K, Yamashita T, Aoki N, Toyama H, Adachi O (1999). "Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5." Biochemistry 38(19);6111-8. PMID: 10320337

Oubrie02: Oubrie A, Rozeboom HJ, Kalk KH, Huizinga EG, Dijkstra BW (2002). "Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer." J Biol Chem 277(5);3727-32. PMID: 11714714

Toyama95: Toyama H, Fujii A, Matsushita K, Shinagawa E, Ameyama M, Adachi O (1995). "Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols." J Bacteriol 177(9);2442-50. PMID: 7730276


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Wed Dec 17, 2014, BIOCYC14B.