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Literature summary for 4.2.1.84 extracted from

  • Stein, N.; Gumataotao, N.; Hajnas, N.; Wu, R.; Lankathilaka, K.P.W.; Bornscheuer, U.T.; Liu, D.; Fiedler, A.T.; Holz, R.C.; Bennett, B.
    Multiple states of nitrile hydratase from Rhodococcus equi TG328-2 structural and mechanistic insights from electron paramagnetic resonance and density functional theory studies (2017), Biochemistry, 56, 3068-3077 .
    View publication on PubMedView publication on EuropePMC
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Metals/Ions

Metals/Ions Comment Organism Structure
Fe3+ the enzyme contains an Fe(III) ion coordinated in a characteristic claw setting by an axial cysteine thiolate, two equatorial peptide nitrogens, the sulfur atoms of equatorial cysteine-sulfenic and cysteine-sulfinic acids, and an axial water/hydroxyl moiety. The cysteine-sulfenic acid is susceptible to oxidation, and the enzyme is traditionally prepared using butyric acid as an oxidative protectant. The as-prepared enzyme exhibits a complex electron paramagnetic resonance spectrum due to multiple low-spin (S = 1/2) Fe(III) species Rhodococcus equi

Organism

Organism UniProt Comment Textmining
Rhodococcus equi
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Rhodococcus equi TG328-2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information structural and mechanistic insights from electron paramagnetic resonance and density functional theory studies Rhodococcus equi ?
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additional information structural and mechanistic insights from electron paramagnetic resonance and density functional theory studies Rhodococcus equi TG328-2 ?
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