View in Gene3D

CATH Superfamily 3.40.50.1820

Alpha/Beta hydrolase fold, catalytic 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: 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.
« Back to all FunFams

FunFam 115235: Triacylglycerol lipase

There are 4 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
Triacylglycerol lipase. [EC: 3.1.1.3]
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate.
  • The pancreatic enzyme acts only on an ester-water interface; the outer ester links are preferentially hydrolyzed.
 390 A0A031GJE5 A0A031GJE5 A0A060L3K4 A0A060L3K4 A0A068FJV4 A0A068FJV4 A0A069BB28 A0A069BB28 A0A084TCY6 A0A084TCY6
(380 more...)
Carboxylesterase. [EC: 3.1.1.1]
A carboxylic ester + H(2)O = an alcohol + a carboxylate.
  • Wide specificity; also hydrolyzes vitamin A esters.
  • The enzymes from microsomes also catalyze the reactions of EC 3.1.1.2, EC 3.1.1.5, EC 3.1.1.6, EC 3.1.1.23, EC 3.1.1.28, EC 3.1.2.2, EC 3.5.1.4, and EC 3.5.1.13.
  • Formerly EC 3.1.1.12.
 8 A0A172PCR4 A0A172PCR4 B3GVV8 B3GVV8 H2D5P3 H2D5P3 I3WE68 I3WE68
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.
 4 A8T1Z7 A8T1Z7 C9YDZ4 C9YDZ4
Lipoyl synthase. [EC: 2.8.1.8]
Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl- L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N(6)- (lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.
  • Member of the 'AdoMet radical' (radical SAM) family, all members of which produce the 5'-deoxyadenosin-5'-yl radical and methionine from AdoMet (i.e. S-adenosylmethionine, or S-(5'-deoxyadenosin- 5'-yl)methionine), by the addition of an electron from an iron-sulfur center.
  • The radical is converted into 5'-deoxyadenosine when it abstracts a hydrogen atom from C-6 and C-8, leaving reactive radicals at these positions so that they can add sulfur, with inversion of configuration.
  • Catalyzes the final step in the de-novo biosynthesis of the lipoyl cofactor, with the other enzyme involved being EC 2.3.1.181.
  • Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein.
  • Examples of such lipoylated proteins include pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein).
  • An alternative lipoylation pathway involves EC 2.7.7.63, which can lipoylate apoproteins using exogenous lipoic acid (or its analogs).
 2 J7JJG8 J7JJG8