Literature summary for 5.4.99.7 extracted from

Chang, C.H.; Chen, Y.C.; Tseng, S.W.; Liu, Y.T.; Wen, H.Y.; Li, W.H.; Huang, C.Y.; Ko, C.Y.; Wang, T.T.; Wu, T.K.
The cysteine 703 to isoleucine or histidine mutation of the oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae generates an iridal-type triterpenoid (2012), Biochimie, 94, 2376-2381.

Search for more literature for 5.4.99.7

Application

Application	Comment	Organism
synthesis	engineering ERG7 for producing biological active agents is promising	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
C703D	site-directed mutagenesis, the mutant shows unaltered product spectrum compared to the wild-type enzyme	Saccharomyces cerevisiae
C703G	site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, but not as diverse as mutants C703I and C703H	Saccharomyces cerevisiae
C703H	site-directed mutagenesis, the mutant generates an unusual truncated bicyclic rearranged intermediate, (8R,9R,10R)-polypoda-5,13E,17E,21-tetraen-3beta-ol, related to iridal-skeleton triterpenoid. Numerous oxidosqualene-cyclized truncated intermediates, including tricyclic, unrearranged tetracyclic with 17alpha/beta exocyclic hydrocarbon side chain, rearranged tetracyclic, and chair-chair-chair tricyclic intermediates, are also isolated from the mutant	Saccharomyces cerevisiae
C703I	site-directed mutagenesis, the mutant generates an unusual truncated bicyclic rearranged intermediate, (8R,9R,10R)-polypoda-5,13E,17E,21-tetraen-3beta-ol, related to iridal-skeleton triterpenoid. Numerous oxidosqualene-cyclized truncated intermediates, including tricyclic, unrearranged tetracyclic with 17alpha/beta exocyclic hydrocarbon side chain, rearranged tetracyclic, and chair-chair-chair tricyclic intermediates, are also isolated from the mutant	Saccharomyces cerevisiae
C703N	site-directed mutagenesis, the mutant shows unaltered product spectrum compared to the wild-type enzyme	Saccharomyces cerevisiae
C703S	site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, but not as diverse as mutants C703I and C703H	Saccharomyces cerevisiae
C703T	site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, but not as diverse as mutants C703I and C703H	Saccharomyces cerevisiae
C703V	site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, but not as diverse as mutants C703I and C703H	Saccharomyces cerevisiae
F699A/C703I	site-directed mutagenesis, inactive mutant	Saccharomyces cerevisiae
F699M/C703I	site-directed mutagenesis, inactive mutant	Saccharomyces cerevisiae
F699T/C703I	site-directed mutagenesis, different oxidosqualene-cyclized truncated intermediates, including tricyclic, unrearranged tetracyclic with 17alpha/beta exocyclic hydrocarbon side chain, rearranged tetracyclic, and chair-chair-chair tricyclic intermediates, are isolated from the mutant	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
(3S)-2,3-epoxy-2,3-dihydrosqualene	Saccharomyces cerevisiae	-	lanosterol	-	?

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	gene ERG7	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(3S)-2,3-epoxy-2,3-dihydrosqualene	-	Saccharomyces cerevisiae	lanosterol	-	?

Synonyms

Synonyms	Comment	Organism
ERG7	-	Saccharomyces cerevisiae
OSC	-	Saccharomyces cerevisiae
Oxidosqualene-lanosterol cyclase	-	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
physiological function	functional role of the Cys703 residue in stabilizing the bicyclic C-8 cation and the rearranged intermediate or interacting with Phe699	Saccharomyces cerevisiae

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)