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| Description | Dehydratation of Ser/Thr residues to Dha/Dhb in the biosynthetic pathway of nosiheptide, after NosIJK-catalyzed addition of MIA. Current knowledge indicates that the full leader peptide is required for substrate recognition. |
| Tailoring |
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| Database References | No database crosslinks available |
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| Metadata |
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| Substrate 1 |
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| Product 1 |
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| Description | Dehydratation of Ser/Thr residues to Dha/Dhb in the biosynthetic pathway of nosiheptide, without attached MIA heterocycle (in vitro reaction). Current knowledge indicates that the full leader peptide is required for substrate recognition. |
| Tailoring |
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| Database References | No database crosslinks available |
| Evidence |
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| References |
| Metadata |
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| Substrate 1 |
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| Product 1 |
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| Accession ID | MITE0000257 |
| Entry Status | Status: active |
| Enzyme Name | NosE |
| Enzyme Description | Dehydratase |
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| Comment | NosE dehydrates Ser/Thr residues together with NosD analogous to the lanthipeptide dehydratase LanB. MIA-addition by NosIJK increases catalytic efficiency but is not essential. |
| Enzyme Visualization (AlphaFold-predicted) |
Version 1 (2025-12-30)
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Auxiliary Enzyme #1
| Enzyme Name | NosD |
| Description | Dehydratase |
| Database References |
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