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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 63127: Probable tryptophanase

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
Tryptophanase. [EC: 4.1.99.1]
L-tryptophan + H(2)O = indole + pyruvate + NH(3).
  • The enzyme cleaves a carbon-carbon bond, releasing indole 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.
  • Also catalyzes 2,3-elimination and beta-replacement reactions of some indole-substituted tryptophan analogs of L-cysteine, L-serine and other 3-substituted amino acids.
 2152 A0A011ANP9 A0A011ANP9 A0A017H5H4 A0A017H5H4 A0A017I469 A0A017I469 A0A017RVR8 A0A017RVR8 A0A023E1V5 A0A023E1V5
(2142 more...)
Tyrosine phenol-lyase. [EC: 4.1.99.2]
L-tyrosine + H(2)O = phenol + pyruvate + NH(3).
  • The enzyme cleaves a carbon-carbon bond, releasing phenol 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 also slowly catalyzes similar reactions with D-tyrosine, S-methyl-L-cysteine, L-cysteine, L-serine and D-serine.
 552 A0A011A172 A0A011A172 A0A017H5N0 A0A017H5N0 A0A023V8R3 A0A023V8R3 A0A037Z355 A0A037Z355 A0A062V115 A0A062V115
(542 more...)