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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_3_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 62: Cystathionine beta-lyase

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
Cysteine-S-conjugate beta-lyase. [EC: 4.4.1.13]
An L-cysteine-S-conjugate + H(2)O = RSH + NH(3) + pyruvate.
  • A pyridoxal 5'-phosphate protein.
  • The enzyme is promiscuous regarding the moiety conjugated to L-cysteine, and can accept both aliphatic and aromatic substitutions.
  • The enzyme cleaves a carbon-sulfur bond, releasing a thiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia.
  • While bacteria and plants have dedicated enzymes, all of the animal enzymes discovered thus far are bifunctional, most of which also act as aminotransferases.
  • Formerly EC 4.4.1.6 and EC 4.4.1.8.
 653 A0A070SYC7 A0A070SYC7 A0A070SYC7 A0A070SYC7 A0A070SYC7 A0A070SYC7 A0A070SYC7 A0A070SYC7 A0A070SYC7 A0A070SYC7
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L-cysteine desulfidase. [EC: 4.4.1.28]
L-cysteine + H(2)O = sulfide + NH(3) + pyruvate.
  • The enzyme from the archaeon Methanocaldococcus jannaschii contains a [4Fe-4S] cluster and is specific for L-cysteine (cf. EC 4.4.1.1).
  • It cleaves a carbon-sulfur bond releasing sulfide and the unstable enamine product 2-aminoprop-2-enoate that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia.
  • The same reaction can also be catalyzed by some pyridoxal-phosphate proteins (cf. EC 4.4.1.1).
 169 A0A070SYC7 A0A070SYC7 A0A070SYC7 A0A070SYC7 A0A070SYC7 A0A070SYC7 A0A070SYC7 A0A070SYC7 A0A070SYC7 A0A070SYC7
(159 more...)