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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.5.1.109 - brevianamide F prenyltransferase (deoxybrevianamide E-forming) and Organism(s) Aspergillus sp. and UniProt Accession E0Y3X1

for references in articles please use BRENDA:EC2.5.1.109
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme from the fungus Aspergilus sp. MF297-2 is specific for brevianamide F , while the enzyme from Aspergillus versicolor accepts a broad range of trytophan-containing cyclic dipeptides . Involved in the biosynthetic pathways of several indole alkaloids such as paraherquamides and malbrancheamides.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Aspergillus sp.
UNIPROT: E0Y3X1
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Aspergillus sp.
The enzyme appears in selected viruses and cellular organisms
Synonyms
brept, cyclic dipeptide c7-prenyltransferase, cdpc7pt, brevianamide f reverse prenyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
brevianamide F reverse prenyltransferase
-
deoxybrevianamide E synthase
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
dimethylallyl-diphosphate:brevianamide-F tert-dimethylallyl-C-2-transferase
The enzyme from the fungus Aspergilus sp. MF297-2 is specific for brevianamide F [1], while the enzyme from Aspergillus versicolor accepts a broad range of trytophan-containing cyclic dipeptides [2]. Involved in the biosynthetic pathways of several indole alkaloids such as paraherquamides and malbrancheamides.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
show the reaction diagram
the enzyme is involved in the alkaloid biosynthetic pathway
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
enzyme activity is independent of divalent cation, although addition of 5 mM Mg2+, Ca2+ or Mn2+ slightly enhances catalysis (about 100-120%)
Mg2+
enzyme activity is independent of divalent cation, although addition of 5 mM Mg2+, Ca2+ or Mn2+ slightly enhances catalysis (about 100-120%)
Mn2+
enzyme activity is independent of divalent cation, although addition of 5 mM Mg2+, Ca2+ or Mn2+ slightly enhances catalysis (about 100-120%)
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
5 mM, about 90% loss of activity
Fe2+
5 mM, about 65% loss of activity
Sn2+
5 mM, about 90% loss of activity
Zn2+
5 mM, about 90% loss of activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00433
brevianamide F
pH 7.5, 22°C
0.00131
dimethylallyl diphosphate
pH 7.5, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.32
brevianamide F
pH 7.5, 22°C
0.42
dimethylallyl diphosphate
pH 7.5, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
73
brevianamide F
pH 7.5, 22°C
320
dimethylallyl diphosphate
pH 7.5, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
pH 5.0: about 50% of maximal activity, pH 10.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
20-40: maximal activity, 50°C: about 30% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
292000
gel filtration
53600
x * 53600, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 53600, calculated from sequence
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E108D
mutant loses at least 92% of its activity
E108G
mutant loses at least 92% of its activity
R122G
mutant with less than 2% catalytic activity
R122H
mutant with less than 2% catalytic activity
W424G
mutant loses more than 98% of its activity
W424Y
mutant retains about 25% of its activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ding, Y.; de Wet, J.R.; Cavalcoli, J.; Li, S.; Greshock, T.J.; Miller, K.A.; Finefield, J.M.; Sunderhaus, J.D.; McAfoos, T.J.; Tsukamoto, S.; Williams, R.M.; Sherman, D.H.
Genome-based characterization of two prenylation steps in the assembly of the stephacidin and notoamide anticancer agents in a marine-derived Aspergillus sp.
J. Am. Chem. Soc.
132
12733-12740
2010
Aspergillus sp. (E0Y3X1)
Manually annotated by BRENDA team