Literature summary for 3.5.1.77 extracted from

Chen, H.; Lin, K.; Lu, C.
Refolding and activation of recombinant N-carbamoyl-D-amino acid amidohydrolase from Escherichia coli inclusion bodies (2005), Process Biochem., 40, 2135-2141.

No PubMed abstract available

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Organism

Organism	UniProt	Comment	Textmining
Agrobacterium tumefaciens	-	plasmid cloned in Escherichia coli	-

Purification (Commentary)

Purification (Comment)	Organism
denatured recombinant enzyme	Agrobacterium tumefaciens

Renatured (Commentary)

Renatured (Comment)	Organism
refolding of purified denatured DCaseH is best yielded at 50% glycerol for 3 days with a 20% renaturation yield. Approximately 38% of the native secondary structure is reformed. The refolding with the addition of glycerol partially recovers both the activity and the native-like secondary structure of the denatured enzyme	Agrobacterium tumefaciens

Synonyms

Synonyms	Comment	Organism
N-carbamoyl-D-amino acid amidohydrolase	-	Agrobacterium tumefaciens

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Release 2023.1 (January 2023)