Literature summary for 1.21.3.1 extracted from

Loke, P.; Sim, T.S.
Site-directed mutagenesis of proline-285 to leucine in Cephalosporium acremonium isopenicillin N-synthase affects catalysis and increases soluble expression at higher temperatures (2001), Z. Naturforsch. C, 56, 413-415.

Search for more literature for 1.21.3.1

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant in Escherichia coli, evaluation of growth temperature for expression of the soluble mutant and wild-type in the Escherichia coli host BL21 (DE3)	Acremonium chrysogenum

Protein Variants

Protein Variants	Comment	Organism
P285L	site-directed mutagenesis, complete loss of activity, increased soluble expression in Escherichia coli host	Acremonium chrysogenum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2	Acremonium chrysogenum	common step in the biosynthesis of penicillins, cephalosporins and cephamycins	isopenicillin N + 2 H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Acremonium chrysogenum	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2	-	Acremonium chrysogenum	isopenicillin N + 2 H2O	-	?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2	common step in the biosynthesis of penicillins, cephalosporins and cephamycins	Acremonium chrysogenum	isopenicillin N + 2 H2O	-	?

Synonyms

Synonyms	Comment	Organism
IPNS	-	Acremonium chrysogenum
isopenicillin N-synthase	-	Acremonium chrysogenum

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Release 2023.1 (January 2023)