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Literature summary extracted from

  • Vitali, J.; Singh, A.K.; Colaneri, M.J.
    Characterization of the dihydroorotase from Methanococcus jannaschii (2017), Protein J., 36, 361-373 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.2.3 gene pyrC, recombinant enzyme expression in Escherichia coli strain Rosetta-gami 2(DE3), subcloning in Escherichia coli strain DH5alpha Methanocaldococcus jannaschii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.2.3 additional information
-
 additional information Michaelis-Menten kinetic analysis, recombinant enzyme Methanocaldococcus jannaschii
3.5.2.3 0.14
-
 (S)-dihydroorotate pH 8.3, 25°C, recombinant enzyme Methanocaldococcus jannaschii
3.5.2.3 0.15
-
 (S)-dihydroorotate pH 8.3, 45°C, recombinant enzyme Methanocaldococcus jannaschii
3.5.2.3 0.52
-
 (S)-dihydroorotate pH 8.3, 80°C, recombinant enzyme Methanocaldococcus jannaschii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.2.3 Zn2+ a zinc-dependent metalloenzyme, average of 2.05 mol zinc per mol protein classifying the Methanocaldococcus jannaschii DHOase as a two-zinc center protein Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.2.3 (S)-dihydroorotate + H2O Methanocaldococcus jannaschii
-
 N-carbamoyl-L-aspartate
-
 r
3.5.2.3 (S)-dihydroorotate + H2O Methanocaldococcus jannaschii ATCC 624773
-
 N-carbamoyl-L-aspartate
-
 r
3.5.2.3 N-carbamoyl-L-aspartate Methanocaldococcus jannaschii
-
 (S)-dihydroorotate + H2O
-
 r
3.5.2.3 N-carbamoyl-L-aspartate Methanocaldococcus jannaschii ATCC 624773
-
 (S)-dihydroorotate + H2O
-
 r

Organism

EC Number Organism UniProt Comment Textmining
3.5.2.3 Methanocaldococcus jannaschii
-
 i.e. Methanococcus jannaschii
-
3.5.2.3 Methanocaldococcus jannaschii ATCC 624773
-
 i.e. Methanococcus jannaschii
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.2.3 recombinant enzyme from Escherichia coli by heat treatment at 85°C for 15 min, dialysis, cation exchange chromatography, and hydrophobic interaction chromatography Methanocaldococcus jannaschii

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.2.3 additional information optimal growth of the organism of 85°C Methanocaldococcus jannaschii
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.2.3 (S)-dihydroorotate + H2O
-
 Methanocaldococcus jannaschii N-carbamoyl-L-aspartate
-
 r
3.5.2.3 (S)-dihydroorotate + H2O
-
 Methanocaldococcus jannaschii ATCC 624773 N-carbamoyl-L-aspartate
-
 r
3.5.2.3 N-carbamoyl-L-aspartate
-
 Methanocaldococcus jannaschii (S)-dihydroorotate + H2O
-
 r
3.5.2.3 N-carbamoyl-L-aspartate
-
 Methanocaldococcus jannaschii ATCC 624773 (S)-dihydroorotate + H2O
-
 r

Subunits

EC Number Subunits Comment Organism
3.5.2.3 ? x * 47503-48104, sequence calculation, mass spectrometry, and SDS-PAGE Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
3.5.2.3 DHOase
-
 Methanocaldococcus jannaschii
3.5.2.3 pyrC
-
 Methanocaldococcus jannaschii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.2.3 25 80 assay at Methanocaldococcus jannaschii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.2.3 85 90 purified recombinant enzyme, 160 min, stable Methanocaldococcus jannaschii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.2.3 8 8.3 assay at Methanocaldococcus jannaschii

General Information

EC Number General Information Comment Organism
3.5.2.3 metabolism catalyzes the conversion of N-carbamoyl-L-aspartate to dihydroorotate in the third step of the de novo biosynthesis of pyrimidines Methanocaldococcus jannaschii
3.5.2.3 additional information structure homology modelling using the structure of DHOase from Methanocaldococcus jannaschii strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440, UniProt ID Q58885. Sequence and structure comparisons Methanocaldococcus jannaschii