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CATH Superfamily 3.40.640.10

Type I PLP-dependent aspartate aminotransferase-like (Major domain)

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Type I PLP-dependent aspartate aminotransferase-like (Major 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 44707: Maltose regulon modulator MalY

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
Cystathionine beta-lyase. [EC: 4.4.1.8]
L-cystathionine + H(2)O = L-homocysteine + NH(3) + pyruvate.
  • The enzyme cleaves a carbon-sulfur bond, releasing L-homocysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia.
  • The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10.
  • The enzyme from some sources also acts on L-cystine, forming pyruvate, ammonia and cysteine persulfide, and a number of related compounds.
  • Possibly identical, in Saccharomyces cerevisiae, with EC 4.4.1.6.
 233 A0A017IFF1 A0A023YXN2 A0A025CQY9 A0A027U0F0 A0A028AKN5 A0A028EB82 A0A029HYG5 A0A029ISG8 A0A029KUN6 A0A029KZG9
(223 more...)
Aspartate transaminase. [EC: 2.6.1.1]
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
  • Also acts on L-tyrosine, L-phenylalanine and L-tryptophan.
  • This activity can be formed from EC 2.6.1.57 by controlled proteolysis.
 1 B7LQP8
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