To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...] View this page in https
ENZYME entry: EC 18.104.22.168
View entry in original ENZYME format
View entry in raw text format (no links)
in this entry
|L-asparagine + 2-oxoglutarate + O(2) <=> (2S,3S)-3-hydroxyasparagine + succinate + CO(2)|
- The enzyme is only able to hydroxylate free L-asparagine.
- It is not active toward D-asparagine.
- The beta-hydroxylated asparagine produced is incorporated at position
9 of the calcium-dependent antibiotic (CDA), an 11-residue non-
ribosomally synthesized acidic lipopeptide lactone.
- Formerly EC 1.14.11.n1.
|PRIAM enzyme-specific profiles||22.214.171.124|
|KEGG Ligand Database for Enzyme Nomenclature||126.96.36.199|
|IUBMB Enzyme Nomenclature||188.8.131.52|
|MEDLINE||Find literature relating to 184.108.40.206|
, with possibility to download in different formats, align etc.
entries corresponding to 1.14.11.-
entries corresponding to 1.14.-.-
entries corresponding to 1.-.-.-