Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

5.4.99.39: beta-amyrin synthase

This is an abbreviated version!
For detailed information about beta-amyrin synthase, go to the full flat file.

Word Map on EC 5.4.99.39

Reaction

(3S)-2,3-epoxy-2,3-dihydrosqualene
=
beta-amyrin

Synonyms

AMS1, amyrin synthase, B-AS, bAS, BAS-like 2, BAS1, BAS2, beta-amyrin cyclase, beta-amyrin synthase, beta-AS, betaAS, BPY, CbbAS, CrAS, EsBAS, EtAS, GmAMS1, GsAS1, GsAS2, MdOSC1, MtAMY1, multifunctional OSC, ObAS1, OPSC 1, OSC, OSC1, OSC2, OXA1, Oxidosqualene cyclase, PBA, PlgOSC1, PNY, PSY, PtBS, SITTS1, SlTTS1, SvBS

ECTree

     5 Isomerases
         5.4 Intramolecular transferases
             5.4.99 Transferring other groups
                5.4.99.39 beta-amyrin synthase

Engineering

Engineering on EC 5.4.99.39 - beta-amyrin synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C486A
mutant shows 46% activity compared to wild-type (100%), Km similar to wild-type, kcat decreased
C564A
mutant shows 1.6% activity compared to wild-type (100%), Km increased compared to wild-type, kcat highly decreased
D485E
mutant shows no activity
D485N
mutant shows no activity
F413A
site-directed mutagenesis, functional analysis, the mutant shows slightly reduced activity compared to thre wild-type enzyme
F413H
site-directed mutagenesis, functional analysis, the mutant shows slightly increased activity compared to thre wild-type enzyme
F413M
site-directed mutagenesis, functional analysis, the mutant shows slightly reduced activity compared to thre wild-type enzyme
F413S
site-directed mutagenesis, functional analysis, the mutant shows slightly increased activity compared to thre wild-type enzyme
F413T
site-directed mutagenesis, functional analysis, the mutant shows slightly increased activity compared to thre wild-type enzyme
F413V
site-directed mutagenesis, functional analysis, the mutant shows slightly reduced activity compared to thre wild-type enzyme
F413W
site-directed mutagenesis, functional analysis, the mutant shows slightly increased activity compared to thre wild-type enzyme
F413Y
site-directed mutagenesis, functional analysis, the mutant shows slightly reduced activity compared to thre wild-type enzyme
F474A
site-directed mutagenesis, the mutant produces significantly larger amounts of the bicyclic products and a decreased amount of beta-amyrin compared to wild-type. The mutant variant produces (9betaH)-polypoda-7,13,17,21-tetraen-3beta-ol and (9betaH)-polypoda-8(26),13,17,21-tetraen-3beta-ol, which are generated from a chair-boat folding conformation
F474G
site-directed mutagenesis, the mutant produces significantly larger amounts of the bicyclic products and a decreased amount of beta-amyrin compared to wild-type
F474H
site-directed mutagenesis
F474L
site-directed mutagenesis, the mutant shows a significantly decreased production of bicyclic compounds, and in turn exhibits a higher production of beta-amyrin compared to wild-type
F474M
site-directed mutagenesis, the mutant shows a significantly decreased production of bicyclic compounds, and in turn exhibits a higher production of beta-amyrin compared to wild-type
F474T
site-directed mutagenesis
F474V
site-directed mutagenesis, the mutant shows a significantly decreased production of bicyclic compounds, and in turn exhibits a higher production of beta-amyrin compared to wild-type
F474W
site-directed mutagenesis
F474Y
site-directed mutagenesis
F728A
highly reduced activity compared to wild-type
F728H
highly reduced activity compared to wild-type
F728I
highly reduced activity compared to wild-type
F728M
highly reduced activity compared to wild-type
F728W
highly reduced activity compared to wild-type
F728Y
activity comparable to wild-type
M729A
site-directed mutagenesis, the mutant shows a decreased enzymatic activity compared to wild-type and altered roduct distribution ratio
M729F
site-directed mutagenesis, the mutant shows a decreased enzymatic activity compared to wild-type and altered roduct distribution ratio
M729G
site-directed mutagenesis, the mutant shows a decreased enzymatic activity compared to wild-type and altered roduct distribution ratio
M729L
site-directed mutagenesis, the mutant shows an unaltered enzymatic activity compared to wild-type and altered roduct distribution ratio
M729N
site-directed mutagenesis, the mutant shows a decreased enzymatic activity compared to wild-type and altered roduct distribution ratio
M729V
site-directed mutagenesis, the mutant shows a decreased enzymatic activity compared to wild-type and altered roduct distribution ratio
M729W
site-directed mutagenesis, the mutant with the bulky substitution is inactive
V483A
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type, and affords monocyclic camelliol C
V483F
site-directed mutagenesis
V483G
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type, and affords monocyclic camelliol C
V483I
site-directed mutagenesis, the mutant shows unaltered substrate specificity compared to wild-type, and affords beta-amyrin as major product
W534A
site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product
W534F
site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product
W534H
site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product
W534I
site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product
W534M
site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product
W534V
site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product
W534Y
site-directed mutagenesis, the mutant shows significantly decreased enzymatic activity compared to wild-type and provides no aberrantly cyclized product
Y259A
site-directed mutagenesis, functional analysis
Y259F
site-directed mutagenesis, functional analysis
Y259H
site-directed mutagenesis, functional analysis
Y259L
site-directed mutagenesis, functional analysis
Y259V
site-directed mutagenesis, functional analysis
Y259W
site-directed mutagenesis, functional analysis
G257W
site-directed mutagenesis
H560Y
site-directed mutagenesis, the mutation of the key residue of GsAS1 to that of GsAS2 results in 38% increased catalytic efficiency compared to wild-type GsAS1
Y560F
site-directed mutagenesis, the mutation of the key residue of GsAS2 results in 71.15% reduced catalytic efficiency compared to wild-type GsAS2
Y560H
site-directed mutagenesis, the mutation of the key residue of GsAS2 results in 41.3% reduced catalytic efficiency compared to wild-type GsAS2
C262S
-
mutation in region responsible for product differentiation. Like wild-type, mutant produces beta-amyrin as sole product
M258I/W259L
-
mutation in region responsible for product differentiation. Mutant produces 40.5% beta-amyrin, 53.4% lupeol, 3.6% butyrospermol and 2.5% germanicol
W259L
-
mutation in region responsible for product differentiation. Mutant produces 30.3% beta-amyrin, 54.6% lupeol, 3.6% butyrospermol and 3.4% germanicol
Y261H
-
mutation in region responsible for product differentiation. Mutant produces 2.4% lupeol, 13.6% germanicol and 84% of dammara-18(E),21-dien-3beta-ol, dammara-18(Z),21-dien-3beta-ol and dammara-18(28),21-dien-3beta-ol
additional information