1996
DOI: 10.1042/bj3150869
|View full text |Cite
|
Sign up to set email alerts
|

Expression, purification and properties of lycopene cyclase from Erwinia uredovora

Abstract: Lycopene cyclase, an enzyme responsible for the formation of cyclic carotenoids from acyclic precursors has been purified to homogeneity in an active state. The Erwinia uredovora lycopene cyclase gene (crtY) was over-expressed in Escherichia coli. From this recombinant strain the enzyme was purified by immuno-affinity chromatography and its cyclization activity characterized as a two-step reaction in which both sides of the lycopene molecule are cyclized to beta-ionone rings with the monocyclic gamma-carotene … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

1
38
0

Year Published

1996
1996
2018
2018

Publication Types

Select...
6
4

Relationship

1
9

Authors

Journals

citations
Cited by 65 publications
(39 citation statements)
references
References 27 publications
1
38
0
Order By: Relevance
“…Similar to PDS and ZDS, other enzymes involved in carotenoid biosynthesis also contain a conserved FAD binding motif in their N termini, for example, CRTISO, LCY-E, LCY-B, and ZEP, suggesting the involvement of redox balance in these reactions even though they do not involve net electron transfer. This is the case in lycopene b-cyclase, which was active in vitro only in the presence of NADH or NADPH (Schnurr et al, 1996), and carotenoid isomerase, which was dependent on redox driving force (Isaacson et al, 2004). Involvement of FAD in ZEP activity has also been demonstrated (Buch et al, 1996).…”
Section: Involvement Of Orr In the Carotenoid Biosynthetic Pathwaymentioning
confidence: 99%
“…Similar to PDS and ZDS, other enzymes involved in carotenoid biosynthesis also contain a conserved FAD binding motif in their N termini, for example, CRTISO, LCY-E, LCY-B, and ZEP, suggesting the involvement of redox balance in these reactions even though they do not involve net electron transfer. This is the case in lycopene b-cyclase, which was active in vitro only in the presence of NADH or NADPH (Schnurr et al, 1996), and carotenoid isomerase, which was dependent on redox driving force (Isaacson et al, 2004). Involvement of FAD in ZEP activity has also been demonstrated (Buch et al, 1996).…”
Section: Involvement Of Orr In the Carotenoid Biosynthetic Pathwaymentioning
confidence: 99%
“…Lycopene cyclase (CrtY) from Erwiizia was expressed in E. coli, purified in an active form and assayed as described [21]. I n vitm assays were carried out by incubation of about 20 pg CrtY, a soybean lipid suspension containing 1.5 pg purified neurosporene and NADPH (final concentration 5 mM) in 0.5 ml SO mM Tridmalate, pH 6.7.…”
Section: Methodsmentioning
confidence: 99%
“…It was determined that the bacterial-type lycopene cyclase, CRTY, converts all-trans-lycopene to ␤-carotene and does not accept tetra-cis-prolycopene as a substrate (Schnurr et al, 1996). Likewise, it was shown that the plant-type lycopene cyclases efficiently convert all-trans-lycopene to ␤-carotene or ␦-carotene (Cunningham et al, 1993Pecker et al, 1996;Ronen et al, 1999).…”
Section: Requirement For Cis-trans Isomerization For Lycopene Cyclizamentioning
confidence: 99%