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Literature summary for 4.2.1.84 extracted from

  • Zhou, Z.; Hashimoto, Y.; Cui, T.; Washizawa, Y.; Mino, H.; Kobayashi, M.
    Unique biogenesis of high-molecular mass multimeric metalloenzyme nitrile hydratase: intermediates and a proposed mechanism for self-subunit swapping maturation (2010), Biochemistry, 49, 9638-9648.
    View publication on PubMed
Search for more literature for 4.2.1.84

Cloned(Commentary)

Cloned (Comment) Organism
separate expression of L-NHase, NhlAE, an the NhhA-NhlE hybrid mediator complex in Rhodococcus rhodochrous strain ATCC12674 and Rhodococcus fascians DSM43985. Necessity of gene nhhG for functional H-NHase expression Rhodococcus rhodochrous

Protein Variants

Protein Variants Comment Organism
alphaV5L site-directed mutagenesis, exchange in the H-NHase does not influence the catalytic activity or the Co2+ content Rhodococcus rhodochrous

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ incorporation of cobalt into L-NHase depends on the alpha-subunit exchange between cobalt-free, apo-L-NHase and its cobalt-containing mediator, NhlAE, i.e. holo-NhlAE, in a mode of post-translational maturation, i.e. self-subunit swapping. NhlE is recognized as a self-subunit swapping chaperone. Incorporation of cobalt into H-NHase also occurs via self-subunit swapping. Cobalt is inserted into cobalt-free, apo-NhhAG, but not into apo-H-NHase, suggesting that NhhG functions not only as a self-subunit swapping chaperone but also as a metallochaperone. Formation of large-sized complexes during self-subunit swapping in H-NHase. Self-subunit swapping mechanism, detailed overview Rhodococcus rhodochrous

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rhodococcus rhodochrous NhhG forms a complex with the alpha-subunit of H-NHase. NhhAG is very similar to the mediator of L-NHase, NhlAE, which is a heterotrimer complex consisting of the cobalt-containing alpha-subunit of L-NHase and NhlE ?
-
 ?
additional information Rhodococcus rhodochrous J1 NhhG forms a complex with the alpha-subunit of H-NHase. NhhAG is very similar to the mediator of L-NHase, NhlAE, which is a heterotrimer complex consisting of the cobalt-containing alpha-subunit of L-NHase and NhlE ?
-
 ?

Organism

Organism UniProt Comment Textmining
Rhodococcus rhodochrous
-
-
-
Rhodococcus rhodochrous J1
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant L-NHase, NhlAE, and the NhhA-NhlE hybrid mediator complex from Rhodococcus rhodochrous strain ATCC12674 and Rhodococcus fascians DSM43985 by ammonium sulfate fractionation anion exchange chromatography, dialysis, gel filtration, and another step of anion exchange chromatography Rhodococcus rhodochrous

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4
-
 purified recombinant wild-type apo-H-NHase, pH 7.5, 20°C Rhodococcus rhodochrous
2.8
-
 purified recombinant V5L mutant apo-H-NHase, pH 7.5, 20°C Rhodococcus rhodochrous
270
-
 purified recombinant V5L mutant R-H-NHase, pH 7.5, 20°C Rhodococcus rhodochrous
275
-
 purified recombinant wild-type R-H-NHase, pH 7.5, 20°C Rhodococcus rhodochrous

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-cyanopyridine + H2O H-NHase activity Rhodococcus rhodochrous nicotinamide
-
 ?
3-cyanopyridine + H2O H-NHase activity Rhodococcus rhodochrous J1 nicotinamide
-
 ?
additional information NhhG forms a complex with the alpha-subunit of H-NHase. NhhAG is very similar to the mediator of L-NHase, NhlAE, which is a heterotrimer complex consisting of the cobalt-containing alpha-subunit of L-NHase and NhlE Rhodococcus rhodochrous ?
-
 ?
additional information NhhG forms a complex with the alpha-subunit of H-NHase. NhhAG is very similar to the mediator of L-NHase, NhlAE, which is a heterotrimer complex consisting of the cobalt-containing alpha-subunit of L-NHase and NhlE Rhodococcus rhodochrous J1 ?
-
 ?

Subunits

Subunits Comment Organism
More NhhG forms a complex with the alpha-subunit of H-NHase. NhhAG is very similar to the mediator of L-NHase, NhlAE, which is a heterotrimer complex consisting of the cobaltcontaining alpha-subunit of L-NHase and NhlE. Formation of large-sized complexes during self-subunit swapping in H-NHase. Self-subunit swapping mechanisms, detailed overview Rhodococcus rhodochrous

Synonyms

Synonyms Comment Organism
H-NHase
-
 Rhodococcus rhodochrous
high-molecular mass nitrile hydratase
-
 Rhodococcus rhodochrous
L-Nhase
-
 Rhodococcus rhodochrous
low-molecular mass nitrile hydratase
-
 Rhodococcus rhodochrous

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
 H-NHase activity assay at Rhodococcus rhodochrous

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 H-NHase activity assay at Rhodococcus rhodochrous

General Information

General Information Comment Organism
additional information incorporation of cobalt into L-NHase in a mode of post-translational maturation, i.e. self-subunit swapping. NhlE is recognized as a self-subunit swapping chaperone, mechanism, detailed overview Rhodococcus rhodochrous