Enzyme

Download
EC Tree
     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.87
Description:Octopamine dehydratase.

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.87
BRENDA Enzyme Link: BRENDA 4.2.1.87
KEGG Enzyme Link: KEGG4.2.1.87
BioCyc Enzyme Link: BioCyc 4.2.1.87
ExPASy Enzyme Link: ExPASy4.2.1.87
EC2PDB Enzyme Link: EC2PDB 4.2.1.87
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.87
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.87
IntEnz Enzyme Link: IntEnz 4.2.1.87
MEDLINE Enzyme Link: MEDLINE 4.2.1.87
MSA:

4.2.1.87;

Phylogenetic Tree:

4.2.1.87;

Uniprot:
M-CSA:
RHEA:18173 (2R)-1-(4-hydroxyphenyl)-2-aminoethanol = (4-hydroxyphenyl)acetaldehyde + NH4(+)
RULE(radius=1) [*:1]-[CH;+0:2](-[OH;+0:3])-[CH2;+0:4]-[NH2;+0:5]>>[*:1]-[CH2;+0:2]-[CH;+0:4]=[O;H0;+0:3].[NH3;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Phosphorylation of farnesol in rat liver microsomes: properties of farnesol kinase and farnesyl phosphate kinase.Bentinger M, Grünler J, Peterson E, Swiezewska E, Dallner G1998 May 159606952
Farnesol kinase is involved in farnesol metabolism, ABA signaling and flower development in Arabidopsis.Fitzpatrick AH, Bhandari J, Crowell DN2011 Jun21395888
Initial catabolism of aromatic biogenic amines by Pseudomonas aeruginosa PAO: pathway description, mapping of mutations, and cloning of essential genes.Cuskey SM, Peccoraro V, Olsen RH1987 Jun3034855
Physiological functions and pharmacological and toxicological effects of p-octopamine.Stohs SJ2015 Jan24654910