4,4'-Diapophytoene desaturase

4,4'-Diapophytoene desaturase (EC 1.3.8.2, dehydrosqualene desaturase, CrtN, 4,4'-diapophytoene:FAD oxidoreductase) is an enzyme with systematic name 15-cis-4,4'-diapophytoene:FAD oxidoreductase. This enzyme catalyses the following chemical reaction

15-cis-4,4'-diapophytoene + 4 FAD

\rightleftharpoons

all-trans-4,4'-diapolycopene + 4 FADH2 (overall reaction)

(1a) 15-cis-4,4'-diapophytoene + FAD

\rightleftharpoons

all-trans-4,4'-diapophytofluene + FADH2

(1b) all-trans-4,4'-diapophytofluene + FAD

\rightleftharpoons

all-trans-4,4'-diapo-zeta-carotene + FADH2

(1c) all-trans-4,4'-diapo-zeta-carotene + FAD

\rightleftharpoons

all-trans-4,4'-diaponeurosporene + FADH2

(1d) all-trans-4,4'-diaponeurosporene + FAD

\rightleftharpoons

all-trans-4,4'-diapolycopene + FADH2

This enzyme is typical of Staphylococcus aureus and some other bacteria such as Heliobacillus sp.

References

Wieland B, Feil C, Gloria-Maercker E, Thumm G, Lechner M, Bravo JM, Poralla K, Götz F (December 1994). "Genetic and biochemical analyses of the biosynthesis of the yellow carotenoid 4,4'-diaponeurosporene of Staphylococcus aureus". Journal of Bacteriology. 176 (24): 7719–26. doi:10.1128/JB.176.24.7719-7726.1994. PMC 197231. PMID 8002598.
Raisig A, Sandmann G (October 1999). "4,4'-diapophytoene desaturase: catalytic properties of an enzyme from the C₃₀ carotenoid pathway of Staphylococcus aureus". Journal of Bacteriology. 181 (19): 6184–7. doi:10.1128/JB.181.19.6184-6187.1999. PMC 103650. PMID 10498735.
Raisig A, Sandmann G (September 2001). "Functional properties of diapophytoene and related desaturases of C₃₀ and C₄₀ carotenoid biosynthetic pathways". Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1533 (2): 164–70. doi:10.1016/s1388-1981(01)00154-8. PMID 11566453.

External links

4,4'-diapophytoene+desaturase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Oxidoreductases: CH–CH oxidoreductases (EC 1.3)
1.3.1: NAD/NADP acceptor	Enoyl-acyl carrier protein reductase/Enoyl ACP reductase 7-Dehydrocholesterol reductase Biliverdin reductase 2,4 Dienoyl-CoA reductase Dihydroxymethyloxo-tetrahydroquinoline dehydrogenase
1.3.3: Oxygen acceptor	Dihydroorotate dehydrogenase Coproporphyrinogen III oxidase Protoporphyrinogen oxidase Bilirubin oxidase Acyl-CoA oxidase Dihydrouracil oxidase Tetrahydroberberine oxidase Secologanin synthase Tryptophan alpha,beta-oxidase Pyrroloquinoline-quinone synthase L-galactonolactone oxidase
1.3.5: Quinone	Succinate dehydrogenase SDHA SDHB SDHC SDHD
1.3.99: Other acceptors	Fumarate reductase Butyryl-CoA dehydrogenase Acyl CoA dehydrogenase ACADSB ACADS 5α-reductase SRD5A1 SRD5A2 SRD5A3 Glutaryl-CoA dehydrogenase Isovaleryl coenzyme A dehydrogenase 3-oxo-5beta-steroid 4-dehydrogenase

v t e 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)

Portal:

Biology

Category:

EC 1.3.8