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CATH Superfamily 3.40.50.1100

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: waiting to be named.

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 135: L-serine dehydratase/L-threonine deaminase

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-serine ammonia-lyase. [EC: 4.3.1.17]
L-serine = pyruvate + NH(3).
  • The reaction catalyzed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.13) followed by tautomerization to an imine form and hydrolysis of the C-N bond.
  • The latter reaction, which can occur spontaneously, is also be catalyzed by EC 3.5.99.10.
  • This reaction is also carried out by EC 4.3.1.19 from a number of sources.
  • Formerly EC 4.2.1.13.
 1 P09367
Threonine ammonia-lyase. [EC: 4.3.1.19]
L-threonine = 2-oxobutanoate + NH(3).
  • The reaction catalyzed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.16), followed by tautomerization to an imine form and hydrolysis of the C-N bond.
  • The latter reaction, which can occur spontaneously, is also be catalyzed by EC 3.5.99.10.
  • The enzymes from a number of sources also act on L-serine, cf. EC 4.3.1.17.
  • Formerly EC 4.2.1.16.
 1 P09367
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