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CATH Superfamily 3.30.559.30

Nonribosomal peptide synthetase, condensation domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Nonribosomal peptide synthetase, condensation domain
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 68: L-2-aminoadipate reductase

There are 2 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
L-2-aminoadipate reductase. [EC: 1.2.1.95]
(S)-2-amino-6-oxohexanoate + NADP(+) + AMP + diphosphate = L-2- aminoadipate + NADPH + ATP.
  • This enzyme, characterized from the yeast Saccharomyces cerevisiae, catalyzes the reduction of L-2-aminoadipate to (S)-2-amino-6- oxohexanoate during L-lysine biosynthesis.
  • An adenylation domain activates the substrate at the expense of ATP hydrolysis, and forms L-2-aminoadipate adenylate, which is attached to a peptidyl-carrier protein (PCP) domain.
  • Binding of NADPH results in reductive cleavage of the acyl-S-enzyme intermediate, releasing (S)-2-amino-6-oxohexanoate.
  • Different from EC 1.2.1.31 which catalyzes a similar transformation in the opposite direction without ATP hydrolysis.
 1 P40976
L-aminoadipate-semialdehyde dehydrogenase. [EC: 1.2.1.31]
(S)-2-amino-6-oxohexanoate + NAD(P)(+) + H(2)O = L-2-aminoadipate + NAD(P)H.
  • (S)-2-amino-6-oxohexanoate undergoes a spontaneous dehydration forming the cyclic (S)-2,3,4,5-tetrahydropyridine-2-carboxylate, which serves as a substrate for the hydrogenation reaction.
 1 P40976
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