EC Number   |
General Information |
Reference |
|---|
    4.2.1.84 | evolution |
because of the absence of sequence similarity between the Co- and Fe-type NHase activators, the two types of NHases might be assembled and maturated by different molecular mechanisms |
730224 |
| 4.2.1.84 | evolution |
mass spectrometry of the primary structure of the studied NHases does not reveal any homology to known NHases |
730311 |
| 4.2.1.84 | evolution |
toyocamycin nitrile hydratase is a unique three-subunit member of the nitrile hydratase family |
729257 |
| 4.2.1.84 | metabolism |
hydrolysis mediated by nitrilase, NHase, and amidase is the most common way for nitrile degradation |
-, 728998 |
| 4.2.1.84 | metabolism |
the enzyme is important in the indole-3-acetic acid biosynthesis pathway together with the nitrilase, EC 3.5.5.1, which produces indole-3-amide, but also indole-3-acetic acid , overview |
729043 |
| 4.2.1.84 | more |
in Co-type NHase, the side-chain of alphaThr109, located iin the cysteine cluster region, undergoes a hydrophobic interaction with the side-chain of alphaVal136. The hydroxyl group of residue alphaTyr114, located near the cysteine cluster region, forms hydrogen bonds with the main-chain oxygen atoms of alphaLeu119 and alphaLeu121, via a water molecule |
-, 648457 |
| 4.2.1.84 | more |
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 |
-, 714229 |
| 4.2.1.84 | more |
structural modeling, overview |
-, 729896 |
| 4.2.1.84 | more |
the alpha-subunit is the minimal sequence needed for nitrile hydration providing a simplified scaffold to study the mechanism and posttranslational modification of this important class of catalysts |
729257 |
| 4.2.1.84 | more |
the recombinant enzyme shows almost the same specific activity and other properties as the native enzyme. Structure of the active center of the recombinant enzyme, overview |
-, 729123 |
