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Literature summary for 2.5.1.109 extracted from

  • 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. (2010), J. Am. Chem. Soc., 132, 12733-12740.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Aspergillus sp.

Protein Variants

Protein Variants Comment Organism
E108D mutant loses at least 92% of its activity Aspergillus sp.
E108G mutant loses at least 92% of its activity Aspergillus sp.
R122G mutant with less than 2% catalytic activity Aspergillus sp.
R122H mutant with less than 2% catalytic activity Aspergillus sp.
W424G mutant loses more than 98% of its activity Aspergillus sp.
W424Y mutant retains about 25% of its activity Aspergillus sp.

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ 5 mM, about 90% loss of activity Aspergillus sp.
Fe2+ 5 mM, about 65% loss of activity Aspergillus sp.
Sn2+ 5 mM, about 90% loss of activity Aspergillus sp.
Zn2+ 5 mM, about 90% loss of activity Aspergillus sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00131
-
dimethylallyl diphosphate pH 7.5, 22°C Aspergillus sp.
0.00433
-
brevianamide F pH 7.5, 22°C Aspergillus sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ enzyme activity is independent of divalent cation, although addition of 5 mM Mg2+, Ca2+ or Mn2+ slightly enhances catalysis (about 100-120%) Aspergillus sp.
Mg2+ enzyme activity is independent of divalent cation, although addition of 5 mM Mg2+, Ca2+ or Mn2+ slightly enhances catalysis (about 100-120%) Aspergillus sp.
Mn2+ enzyme activity is independent of divalent cation, although addition of 5 mM Mg2+, Ca2+ or Mn2+ slightly enhances catalysis (about 100-120%) Aspergillus sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53600
-
x * 53600, calculated from sequence Aspergillus sp.
292000
-
gel filtration Aspergillus sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dimethylallyl diphosphate + brevianamide F Aspergillus sp. the enzyme is involved in the alkaloid biosynthetic pathway diphosphate + deoxybrevianamide E
-
?

Organism

Organism UniProt Comment Textmining
Aspergillus sp. E0Y3X1
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dimethylallyl diphosphate + brevianamide F the enzyme is involved in the alkaloid biosynthetic pathway Aspergillus sp. diphosphate + deoxybrevianamide E
-
?
dimethylallyl diphosphate + brevianamide F the enzyme is specific for brevianamide F i.e. (3S,8aS)-3-(1H-indol-3-ylmethyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione Aspergillus sp. diphosphate + deoxybrevianamide E deoxybrevianamide E i.e. (3S,8aS)-3-[[2-(2-methylbut-3-en-2-yl)-1H-indol-3-yl]methyl]-octahydropyrrolo[1,2-a]piperazine-1,4-dione ?

Subunits

Subunits Comment Organism
? x * 53600, calculated from sequence Aspergillus sp.

Synonyms

Synonyms Comment Organism
brevianamide F reverse prenyltransferase
-
Aspergillus sp.
deoxybrevianamide E synthase
-
Aspergillus sp.
NotF
-
Aspergillus sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20 40
-
Aspergillus sp.

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 50 20-40: maximal activity, 50°C: about 30% of maximal activity Aspergillus sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.32
-
brevianamide F pH 7.5, 22°C Aspergillus sp.
0.42
-
dimethylallyl diphosphate pH 7.5, 22°C Aspergillus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 9
-
Aspergillus sp.

pH Range

pH Minimum pH Maximum Comment Organism
5 10 pH 5.0: about 50% of maximal activity, pH 10.0: about 70% of maximal activity Aspergillus sp.

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
73
-
brevianamide F pH 7.5, 22°C Aspergillus sp.
320
-
dimethylallyl diphosphate pH 7.5, 22°C Aspergillus sp.