Literature summary for 5.4.99.39 extracted from

Kushiro, T.; Shibuya, M.; Ebizuka, Y.
Chimeric triterpene synthase. A possible model for multifunctional triterpene synthase (1999), J. Am. Chem. Soc., 121, 1208-1216.

No PubMed abstract available

Search for more literature for 5.4.99.39

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of chimeric proteins using beta-amyrin synthase from Panax ginseng and lupeol synthase from Arabidopsis thaliana. Chimera with N-terminal half of beta-amyrin synthase and C-terminal half of lupeol synthase produces beta-amyrin and lupeol in ratio 3:1. Chimera with only the second quarter of the N-terminus from beta-amyrin synthase, produces beta-amyrin and lupeol in a 4:1 ratio, while another chimera created by mixed PCR produces beta-amyrin and lupeol in a 1:4 ratio	Arabidopsis thaliana

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
(3S)-2,3-epoxy-2,3-dihydrosqualene = beta-amyrin	no scrambling of methyl groups is observed during beta-amyrin formation, the isopropyl group of the lupenyl cation intermediate must be held tightly during product formation	Arabidopsis thaliana	a

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)