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Literature summary extracted from

  • Fan, A.; Chen, H.; Wu, R.; Xu, H.; Li, S.M.
    A new member of the DMATS superfamily from Aspergillus niger catalyzes prenylations of both tyrosine and tryptophan derivatives (2014), Appl. Microbiol. Biotechnol., 98, 10119-10129.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.80 gene An13g01840, DNA and amino acid sequence determination and analysis, overexpression of His6-tagged enzyme in Escherichia coli strain SoluBL21, subcloning in Escherichia coli strain XL1 BlueMRF' Aspergillus niger
2.5.1.122 gene An13g01840, DNA and amino acid sequence determination and analysis, overexpression of His6-tagged enzyme in Escherichia coli strain SoluBL21, subcloning in Escherichia coli strain XL1 BlueMRF' Aspergillus niger

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.80 Cu2+ strong inhibition Aspergillus niger
2.5.1.80 Zn2+ slight inhibition Aspergillus niger
2.5.1.122 Cu2+ strong inhibition Aspergillus niger
2.5.1.122 Zn2+ slight inhibition Aspergillus niger

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.80 0.19
-
 L-tryptophan pH 7.5, 37°C Aspergillus niger
2.5.1.80 0.71
-
 dimethylallyl diphosphate pH 7.5, 37°C Aspergillus niger
2.5.1.122 0.19
-
 L-tryptophan at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.19
-
 3,4-dihydroxy-L-phenylalanine at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.22
-
 D-tyrosine at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.24
-
 L-tyrosine pH 7.5, 37°C Aspergillus niger
2.5.1.122 0.24
-
 L-tyrosine at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.25
-
 4-methyl-DL-tryptophan at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.29
-
 3-iodo-L-tyrosine at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.42
-
 alpha-methyl-L-tyrosine at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.69
-
 4-methyl-DL-tryptophan at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.71
-
 dimethylallyl diphosphate pH 7.5, 37°C Aspergillus niger
2.5.1.122 0.71
-
 dimethylallyl diphosphate with 3-iodo-L-tyrosine as cosubstrate, at pH 7.5 and 37°C Aspergillus niger

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.80 Ca2+ activates Aspergillus niger
2.5.1.80 Mg2+ activates Aspergillus niger
2.5.1.80 additional information no significant effects on enzyme activity by K+, Na+, Mg2+, Mn2+, Co2+, or EDTA Aspergillus niger
2.5.1.122 Ca2+ activates Aspergillus niger
2.5.1.122 Mg2+ activates Aspergillus niger
2.5.1.122 additional information addition of K+, Na+, Mg2+, Mn2+, Co2+, or EDTA to the reaction mixture does not change the enzyme activity significantly Aspergillus niger
2.5.1.122 additional information no significant effects on enzyme activity by K+, Na+, Mg2+, Mn2+, Co2+, or EDTA Aspergillus niger

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.80 52700
-
-
 Aspergillus niger
2.5.1.80 53500
-
-
 Aspergillus niger
2.5.1.80 228000
-
 recombinant His6-tagged enzyme, gel filtration Aspergillus niger
2.5.1.122 52700
-
-
 Aspergillus niger
2.5.1.122 52700
-
 x * 52700, calculated from amino acid sequence Aspergillus niger
2.5.1.122 53500
-
-
 Aspergillus niger
2.5.1.122 228000
-
 recombinant His6-tagged enzyme, gel filtration Aspergillus niger

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.122 dimethylallyl diphosphate + L-tyrosine Aspergillus niger
-
 diphosphate + 4-O-dimethylallyl-L-tyrosine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.80 Aspergillus niger A2R1N3 gene An13g01840 or ANI_1_660114
-
2.5.1.122 Aspergillus niger
-
-
-
2.5.1.122 Aspergillus niger A2R1N3 gene An13g01840 or ANI_1_660114
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.80 recombinant His6-tagged enzyme from Escherichia coli strain BL21 to near homogeneity by nickel affinity chromatography and desalting gel filtration Aspergillus niger
2.5.1.122 recombinant His6-tagged enzyme from Escherichia coli strain BL21 to near homogeneity by nickel affinity chromatography and desalting gel filtration Aspergillus niger

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.5.1.80 mycelium
-
 Aspergillus niger
-
2.5.1.122 mycelium
-
 Aspergillus niger
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.80 dimethylallyl diphosphate + 4-methyl-DL-tryptophan
-
 Aspergillus niger diphosphate + 7-(3-methylbut-2-enyl)-4-methyl-DL-tryptophan
-
 ?
2.5.1.80 dimethylallyl diphosphate + 5-methoxy-DL-tryptophan
-
 Aspergillus niger diphosphate + 7-(3-methylbut-2-enyl)-5-methoxy-DL-tryptophan
-
 ?
2.5.1.80 dimethylallyl diphosphate + 5-methyl-DL-tryptophan
-
 Aspergillus niger diphosphate + 7-(3-methylbut-2-enyl)-5-methyl-DL-tryptophan
-
 ?
2.5.1.80 dimethylallyl diphosphate + 6-methyl-DL-tryptophan
-
 Aspergillus niger diphosphate + 7-(3-methylbut-2-enyl)-6-methyl-DL-tryptophan
-
 ?
2.5.1.80 dimethylallyl diphosphate + L-abrine
-
 Aspergillus niger diphosphate + ?
-
 ?
2.5.1.80 dimethylallyl diphosphate + L-beta-homotryptophan
-
 Aspergillus niger diphosphate + 7-(3-methylbut-2-enyl)-L-beta-homotryptophan
-
 ?
2.5.1.80 dimethylallyl diphosphate + L-tryptophan
-
 Aspergillus niger diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.80 additional information the enzyme catalyzes O-prenylation of L-tyrosine, EC 2.5.1.122, and also accepts 4-amino-L-phenylalanine for an N-prenylation and L-tryptophan for a C7-prenylation, EC 2.5.1.80. HRMS analysis of the enzyme product, overviews. 7-Prenylation substrate specificity, overview. No activity with D-tryptophan Aspergillus niger ?
-
 ?
2.5.1.122 dimethylallyl diphosphate + 3,4-dihydroxy-L-phenylalanine 98% activity compared to 3-iodo-L-tyrosine Aspergillus niger ?
-
 ?
2.5.1.122 dimethylallyl diphosphate + 3,4-dihydroxy-L-phenylalanine
-
 Aspergillus niger diphosphate + ?
-
 ?
2.5.1.122 dimethylallyl diphosphate + 3-fluoro-DL-tyrosine 53% activity compared to 3-iodo-L-tyrosine Aspergillus niger ?
-
 ?
2.5.1.122 dimethylallyl diphosphate + 3-iodo-L-tyrosine 100% activity Aspergillus niger ?
-
 ?
2.5.1.122 dimethylallyl diphosphate + 3-iodo-L-tyrosine
-
 Aspergillus niger diphosphate + ?
-
 ?
2.5.1.122 dimethylallyl diphosphate + 4-amino-L-phenylalanine 23% activity compared to 3-iodo-L-tyrosine Aspergillus niger ?
-
 ?
2.5.1.122 dimethylallyl diphosphate + 4-amino-L-phenylalanine prenylation at 4-O- or N-atom Aspergillus niger diphosphate + 4-dimethylallylamino-L-phenylalanine
-
 ?
2.5.1.122 dimethylallyl diphosphate + 4-methyl-DL-tryptophan 13% activity compared to 3-iodo-L-tyrosine Aspergillus niger ?
-
 ?
2.5.1.122 dimethylallyl diphosphate + 4-methyl-DL-tryptophan 41% activity compared to 3-iodo-L-tyrosine Aspergillus niger diphosphate + 7-dimethylallyl-4-methyl-L-tryptophan
-
 ?
2.5.1.122 dimethylallyl diphosphate + 5-methyl-DL-tryptophan 10% activity compared to 3-iodo-L-tyrosine Aspergillus niger diphosphate + 7-dimethylally-5-methyl-L-tryptophan
-
 ?
2.5.1.122 dimethylallyl diphosphate + alpha-methyl-L-tyrosine 98% activity compared to 3-iodo-L-tyrosine Aspergillus niger ?
-
 ?
2.5.1.122 dimethylallyl diphosphate + D-tyrosine 33% activity compared to 3-iodo-L-tyrosine Aspergillus niger ?
-
 ?
2.5.1.122 dimethylallyl diphosphate + D-tyrosine
-
 Aspergillus niger diphosphate + 4-O-dimethylallyl-D-tyrosine
-
 ?
2.5.1.122 dimethylallyl diphosphate + L-tryptophan 33% activity compared to 3-iodo-L-tyrosine Aspergillus niger diphosphate + 7-dimethylallyl-L-tryptophan
-
 ?
2.5.1.122 dimethylallyl diphosphate + L-tyrosine
-
 Aspergillus niger diphosphate + 4-O-dimethylallyl-L-tyrosine
-
 ?
2.5.1.122 dimethylallyl diphosphate + L-tyrosine 98% activity compared to 3-iodo-L-tyrosine Aspergillus niger diphosphate + 4-O-dimethylallyl-L-tyrosine
-
 ?
2.5.1.122 additional information the enzyme shows a wider substrate spectrum compared to tyrosine prenyltransferase SirD. It catalyzes O-prenylation of L-tyrosine, EC 2.5.1.122, and also accepts 4-amino-L-phenylalanine for an N-prenylation and L-tryptophan for a C7-prenylation, EC 2.5.1.80. It is also active with 4-amino-L-phenylalanine as well as 4- and 5-methyl-DL-tryptophan. HRMS analysis of the enzyme products, overview. 3,5-dibromo-L-tyrosine is a poor substrate Aspergillus niger ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.80 ? x * 53500, recombinant His6-tagged enzyme, SDS-PAGE, x * 52700, about, sequence calculation Aspergillus niger
2.5.1.122 ? x * 52700, calculated from amino acid sequence Aspergillus niger
2.5.1.122 ? x * 53500, recombinant His6-tagged enzyme, SDS-PAGE, x * 52700, about, sequence calculation Aspergillus niger

Synonyms

EC Number Synonyms Comment Organism
2.5.1.80 7-DMATS
-
 Aspergillus niger
2.5.1.80 ANI_1_660114
-
 Aspergillus niger
2.5.1.80 CAK41583
-
 Aspergillus niger
2.5.1.122 ANI_1_660114
-
 Aspergillus niger
2.5.1.122 CAK41583
-
 Aspergillus niger
2.5.1.122 tyrosine O-prenyltransferase
-
 Aspergillus niger
2.5.1.122 TyrPT
-
 Aspergillus niger

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.80 37
-
 assay at Aspergillus niger
2.5.1.122 37
-
 assay at Aspergillus niger

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.80 0.0053
-
 L-tryptophan pH 7.5, 37°C Aspergillus niger
2.5.1.122 0.0036
-
 4-methyl-DL-tryptophan at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.0053
-
 L-tryptophan at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.16
-
 D-tyrosine at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.16
-
 3-iodo-L-tyrosine at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.2
-
 4-methyl-DL-tryptophan at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.26
-
 alpha-methyl-L-tyrosine at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.27
-
 3,4-dihydroxy-L-phenylalanine at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.58
-
 L-tyrosine pH 7.5, 37°C Aspergillus niger
2.5.1.122 0.58
-
 L-tyrosine at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.69
-
 dimethylallyl diphosphate with 3-iodo-L-tyrosine as cosubstrate, at pH 7.5 and 37°C Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.80 7.5
-
 assay at Aspergillus niger
2.5.1.122 7.5
-
 assay at Aspergillus niger

General Information

EC Number General Information Comment Organism
2.5.1.80 evolution the enzyme is a member of the DMATS superfamily Aspergillus niger
2.5.1.122 evolution the enzyme is a member of the DMATS superfamily Aspergillus niger

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.5.1.122 0.028
-
 L-tryptophan at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.043
-
 4-methyl-DL-tryptophan at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.551
-
 3-iodo-L-tyrosine at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.619
-
 alpha-methyl-L-tyrosine at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.727
-
 D-tyrosine at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.8
-
 4-methyl-DL-tryptophan at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 0.972
-
 dimethylallyl diphosphate with 3-iodo-L-tyrosine as cosubstrate, at pH 7.5 and 37°C Aspergillus niger
2.5.1.122 1.421
-
 3,4-dihydroxy-L-phenylalanine at pH 7.5 and 37°C Aspergillus niger