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Literature summary extracted from

  • Liu, Y.; Yan, Z.; Lu, X.; Xiao, D.; Jiang, H.
    Improving the catalytic activity of isopentenyl phosphate kinase through protein coevolution analysis (2016), Sci. Rep., 6, 24117.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.26 gene ipk, recombinant expression of His-tagged codon-optimized wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Methanocaldococcus jannaschii
2.7.4.26 gene ipk, recombinant expression of His-tagged codon-optimized wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Thermoplasma acidophilum
2.7.4.26 gene ipk, recombinant expression of His-tagged codon-optimized wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Methanothermobacter thermautotrophicus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.4.26 A53V site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, the mutant shows increased activity compared to the wild-type enzyme Thermoplasma acidophilum
2.7.4.26 G44A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Thermoplasma acidophilum
2.7.4.26 G45A site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Thermoplasma acidophilum
2.7.4.26 G49A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Thermoplasma acidophilum
2.7.4.26 I140V site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme Thermoplasma acidophilum
2.7.4.26 K204A site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme Thermoplasma acidophilum
2.7.4.26 K204G site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Thermoplasma acidophilum
2.7.4.26 additional information analysis and evaluation of a method of rational design that is able to identify desired mutants by analyzing the coevolution of protein sequence, use for evolving an archaeal isopentenyl phosphate kinase that can convert dimethylallyl alcohol into precursor of isoprenoids, overview. Site-directed mutagenesis of sites idetified as coevolved in the IPK family proteins Thermoplasma acidophilum
2.7.4.26 V130A site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Thermoplasma acidophilum
2.7.4.26 V73I site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme Thermoplasma acidophilum
2.7.4.26 V73I/K204G site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme Thermoplasma acidophilum
2.7.4.26 V73I/Y141V site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme Thermoplasma acidophilum
2.7.4.26 V73I/Y141V/K204G site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme Thermoplasma acidophilum
2.7.4.26 V73T site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Thermoplasma acidophilum
2.7.4.26 Y141L site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Thermoplasma acidophilum
2.7.4.26 Y141V site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme Thermoplasma acidophilum
2.7.4.26 Y141V/K204G site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme Thermoplasma acidophilum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.4.26 Mg2+ required Methanocaldococcus jannaschii
2.7.4.26 Mg2+ required Thermoplasma acidophilum
2.7.4.26 Mg2+ required Methanothermobacter thermautotrophicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.4.26 ATP + dimethylallyl phosphate Methanocaldococcus jannaschii
-
ADP + dimethylallyl diphosphate
-
?
2.7.4.26 ATP + dimethylallyl phosphate Thermoplasma acidophilum
-
ADP + dimethylallyl diphosphate
-
?
2.7.4.26 ATP + dimethylallyl phosphate Methanothermobacter thermautotrophicus
-
ADP + dimethylallyl diphosphate
-
?
2.7.4.26 ATP + dimethylallyl phosphate Methanothermobacter thermautotrophicus DSM 1053
-
ADP + dimethylallyl diphosphate
-
?
2.7.4.26 ATP + dimethylallyl phosphate Methanocaldococcus jannaschii DSM 2661
-
ADP + dimethylallyl diphosphate
-
?
2.7.4.26 ATP + isopentenyl phosphate Methanocaldococcus jannaschii
-
ADP + isopentenyl diphosphate
-
?
2.7.4.26 ATP + isopentenyl phosphate Thermoplasma acidophilum
-
ADP + isopentenyl diphosphate
-
?
2.7.4.26 ATP + isopentenyl phosphate Methanothermobacter thermautotrophicus
-
ADP + isopentenyl diphosphate
-
?
2.7.4.26 ATP + isopentenyl phosphate Methanothermobacter thermautotrophicus DSM 1053
-
ADP + isopentenyl diphosphate
-
?
2.7.4.26 ATP + isopentenyl phosphate Methanocaldococcus jannaschii DSM 2661
-
ADP + isopentenyl diphosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.26 Methanocaldococcus jannaschii Q60352 gene ipk
-
2.7.4.26 Methanocaldococcus jannaschii DSM 2661 Q60352 gene ipk
-
2.7.4.26 Methanothermobacter thermautotrophicus O26153 gene ipk
-
2.7.4.26 Methanothermobacter thermautotrophicus DSM 1053 O26153 gene ipk
-
2.7.4.26 Thermoplasma acidophilum Q9HLX1 gene ipk
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.26 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration Methanocaldococcus jannaschii
2.7.4.26 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration Thermoplasma acidophilum
2.7.4.26 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration Methanothermobacter thermautotrophicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.26 ATP + dimethylallyl alcohol molecular docking analysis indicates that dimethylallyl alcohol is a substrate for the archaeal IPK, although with low activity for the wild-type. The mutant enzymes show increased activity with dimethylallyl alcohol as substrate Thermoplasma acidophilum ADP + dimethylallyl phosphate
-
?
2.7.4.26 ATP + dimethylallyl alcohol molecular docking analysis indicates that dimethylallyl alcohol is a substrate for the archaeal IPK, although with low activity for the wild-type. The mutant enzymes show increased activity with dimethylallyl alcohol as substrate Methanothermobacter thermautotrophicus ADP + dimethylallyl phosphate
-
?
2.7.4.26 ATP + dimethylallyl alcohol molecular docking analysis indicates that dimethylallyl alcohol is a substrate for the archaeal IPK, although with low activity for thwild-type. The mutant enzymes show increased activity with dimethylallyl alcohol as substrate Methanocaldococcus jannaschii ADP + dimethylallyl phosphate
-
?
2.7.4.26 ATP + dimethylallyl alcohol molecular docking analysis indicates that dimethylallyl alcohol is a substrate for the archaeal IPK, although with low activity for the wild-type. The mutant enzymes show increased activity with dimethylallyl alcohol as substrate Methanothermobacter thermautotrophicus DSM 1053 ADP + dimethylallyl phosphate
-
?
2.7.4.26 ATP + dimethylallyl alcohol molecular docking analysis indicates that dimethylallyl alcohol is a substrate for the archaeal IPK, although with low activity for thwild-type. The mutant enzymes show increased activity with dimethylallyl alcohol as substrate Methanocaldococcus jannaschii DSM 2661 ADP + dimethylallyl phosphate
-
?
2.7.4.26 ATP + dimethylallyl phosphate
-
Methanocaldococcus jannaschii ADP + dimethylallyl diphosphate
-
?
2.7.4.26 ATP + dimethylallyl phosphate
-
Thermoplasma acidophilum ADP + dimethylallyl diphosphate
-
?
2.7.4.26 ATP + dimethylallyl phosphate
-
Methanothermobacter thermautotrophicus ADP + dimethylallyl diphosphate
-
?
2.7.4.26 ATP + dimethylallyl phosphate
-
Methanothermobacter thermautotrophicus DSM 1053 ADP + dimethylallyl diphosphate
-
?
2.7.4.26 ATP + dimethylallyl phosphate
-
Methanocaldococcus jannaschii DSM 2661 ADP + dimethylallyl diphosphate
-
?
2.7.4.26 ATP + isopentenyl phosphate
-
Methanocaldococcus jannaschii ADP + isopentenyl diphosphate
-
?
2.7.4.26 ATP + isopentenyl phosphate
-
Thermoplasma acidophilum ADP + isopentenyl diphosphate
-
?
2.7.4.26 ATP + isopentenyl phosphate
-
Methanothermobacter thermautotrophicus ADP + isopentenyl diphosphate
-
?
2.7.4.26 ATP + isopentenyl phosphate
-
Methanothermobacter thermautotrophicus DSM 1053 ADP + isopentenyl diphosphate
-
?
2.7.4.26 ATP + isopentenyl phosphate
-
Methanocaldococcus jannaschii DSM 2661 ADP + isopentenyl diphosphate
-
?

Synonyms

EC Number Synonyms Comment Organism
2.7.4.26 IPK
-
Methanocaldococcus jannaschii
2.7.4.26 IPK
-
Thermoplasma acidophilum
2.7.4.26 IPK
-
Methanothermobacter thermautotrophicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.4.26 37
-
assay at Methanocaldococcus jannaschii
2.7.4.26 37
-
assay at Thermoplasma acidophilum
2.7.4.26 37
-
assay at Methanothermobacter thermautotrophicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.4.26 8
-
assay at Methanocaldococcus jannaschii
2.7.4.26 8
-
assay at Thermoplasma acidophilum
2.7.4.26 8
-
assay at Methanothermobacter thermautotrophicus

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.4.26 ATP
-
Methanocaldococcus jannaschii
2.7.4.26 ATP
-
Thermoplasma acidophilum
2.7.4.26 ATP
-
Methanothermobacter thermautotrophicus

General Information

EC Number General Information Comment Organism
2.7.4.26 metabolism the enzyme is involved in the mevalonate pathway forming the building blocks for isoprenoid biosynthesis, overview Methanocaldococcus jannaschii
2.7.4.26 metabolism the enzyme is involved in the mevalonate pathway forming the building blocks for isoprenoid biosynthesis, overview Thermoplasma acidophilum
2.7.4.26 metabolism the enzyme is involved in the mevalonate pathway forming the building blocks for isoprenoid biosynthesis, overview Methanothermobacter thermautotrophicus