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CATH Superfamily 2.60.40.10

Immunoglobulins

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:

"
Immunoglobulins
".

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 137188: Maltogenic alpha-amylase (Glucan 1,4-alpha-maltohy...

There are 10 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
Alpha-amylase. [EC: 3.2.1.1]
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.
  • Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration.
  • The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.
 698 A0A021VWY7 A0A021VWY7 A0A022MLL8 A0A022MLL8 A0A024YJM4 A0A024YJM4 A0A059XUV5 A0A059XUV5 A0A060S3R1 A0A060S3R1
(688 more...)
Glucan 1,4-alpha-glucosidase. [EC: 3.2.1.3]
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D- glucose.
  • Most forms of the enzyme can rapidly hydrolyze 1,6-alpha-D-glucosidic bonds when the next bond in the sequence is 1,4, and some preparations of this enzyme hydrolyze 1,6- and 1,3-alpha-D-glucosidic bonds in other polysaccharides.
  • This entry covers all such enzymes acting on polysaccharides more rapidly than on oligosaccharides.
  • EC 3.2.1.20 from mammalian intestine can catalyze similar reactions.
 676 A0A010R450 A0A010R450 A0A022WCT2 A0A022WCT2 A0A022Y2Z6 A0A022Y2Z6 A0A024SN40 A0A024SN40 A0A059JGW1 A0A059JGW1
(666 more...)
Cyclomaltodextrin glucanotransferase. [EC: 2.4.1.19]
Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)- alpha-D-glucosidic bond.
  • Cyclomaltodextrins (Schardinger dextrins) of various sizes (6, 7, 8, etc. glucose units) are formed reversibly from starch and similar substrates.
  • Also disproportionates linear maltodextrins without cyclizing (cf. EC 2.4.1.25).
 148 A0A060M208 A0A060M208 A0A078KL18 A0A078KL18 A0A085PJE2 A0A085PJE2 A0A097CPM3 A0A097CPM3 A0A0B0HZ06 A0A0B0HZ06
(138 more...)
Glucan 1,4-alpha-maltotetraohydrolase. [EC: 3.2.1.60]
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends.
  • Compare EC 3.2.1.2, which removes successive maltose residues, and EC 3.2.1.98 and EC 3.2.1.116.
 12 A0A098FZN6 A0A098FZN6 A0A0T8LD37 A0A0T8LD37 A4XX23 A4XX23 P13507 P13507 P22963 P22963
(2 more...)
Beta-amylase. [EC: 3.2.1.2]
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.
  • Acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion.
 12 A0A0C5VGT4 A0A0C5VGT4 A0A0F4QQ25 A0A0F4QQ25 A3YGL7 A3YGL7 D2KFQ6 D2KFQ6 P19584 P19584
(2 more...)
Glucan 1,4-alpha-maltohydrolase. [EC: 3.2.1.133]
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains.
  • Acts on starch and related polysaccharides and oligosaccharides.
  • The product is alpha-maltose; cf. EC 3.2.1.2.
 10 A0A0E3W6L8 A0A0E3W6L8 A0A150M1H3 A0A150M1H3 E6QP40 E6QP40 L8N3W2 L8N3W2 P19531 P19531
4-alpha-glucanotransferase. [EC: 2.4.1.25]
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan.
  • An enzymic activity of this nature forms part of the mammalian and Saccharomyces cerevisiae glycogen branching system (see EC 3.2.1.33).
  • Formerly EC 2.4.1.3.
 6 A0A1B0SZS5 A0A1B0SZS5 Q69Q02 Q69Q02 Q8RXD9 Q8RXD9
1,4-alpha-glucan branching enzyme. [EC: 2.4.1.18]
Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.
  • Converts amylose into amylopectin.
  • The description (official name) requires a qualification depending on the product, glycogen or amylopectin, e.g. glycogen branching enzyme, amylopectin branching enzyme.
  • The latter has frequently been termed Q-enzyme.
 2 K6XSL5 K6XSL5
Glucan 1,4-alpha-maltohexaosidase. [EC: 3.2.1.98]
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non- reducing chain ends.
  • Cf. EC 3.2.1.3, which removes successive glucose residues.
  • Cf. EC 3.2.1.2, which removes successive maltose residues.
  • Cf. EC 3.2.1.116, which removes successive maltotriose residues.
  • Cf. EC 3.2.1.60, which removes successive maltotetraose residues.
  • The products have the alpha-configuration.
 2 A0A099KBI7 A0A099KBI7
Purine nucleosidase. [EC: 3.2.2.1]
A purine nucleoside + H(2)O = D-ribose + a purine base.
  • The enzyme from the bacterium Ochrobactrum anthropi specifically catalyzes the irreversible N-riboside hydrolysis of purine nucleosides.
  • Pyrimidine nucleosides, purine and pyrimidine nucleotides, NAD(+), NADP(+) and nicotinaminde mononucleotide are not substrates.
 2 Q59222 Q59222
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