KEGG   ENZYME: 3.2.1.164Help
Entry
EC 3.2.1.164                Enzyme                                 

Name
galactan endo-1,6-beta-galactosidase;
endo-1,6-beta-galactanase
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
BRITE hierarchy
Sysname
endo-beta-(1->6)-galactanase
Reaction(IUBMB)
Endohydrolysis of (1->6)-beta-D-galactosidic linkages in arabinogalactan proteins and (1->3):(1->6)-beta-galactans to yield galactose and (1->6)-beta-galactobiose as the final products
Comment
The enzyme specifically hydrolyses 1,6-beta-D-galactooligosaccharides with a degree of polymerization (DP) higher than 3, and their acidic derivatives with 4-O-methylglucosyluronate or glucosyluronate groups at the non-reducing terminals [2]. 1,3-beta-D- and 1,4-beta-D-galactosyl residues cannot act as substrates. The enzyme can also hydrolyse alpha-L-arabinofuranosidase-treated arabinogalactan protein (AGP) extracted from radish roots [2,3]. AGPs are thought to be involved in many physiological events, such as cell division, cell expansion and cell death [3].
History
EC 3.2.1.164 created 2007
Orthology
K18579  
galactan endo-1,6-beta-galactosidase
Genes
NCR: 
SMP: 
PAN: 
MTM: 
TRE: 
ELA: 
PTE: 
BZE: 
BSC: 
BOR: 
PIF: 
SUR: 
SMA: 
SCB: 
SVL: 
SDV: 
SCI: 
SRC: 
 » show all
Taxonomy
Reference
1
  Authors
Brillouet, J.-M., Williams, P. and Moutounet, M.
  Title
Purification and some properties of a novel endo-beta-(1->6)-D-galactanase from Aspergillus niger.
  Journal
Agric. Biol. Chem. 55 (1991) 1565-1571.
Reference
2  [PMID:12543554]
  Authors
Okemoto K, Uekita T, Tsumuraya Y, Hashimoto Y, Kasama T.
  Title
Purification and characterization of an endo-beta-(1-->6)-galactanase from Trichoderma viride.
  Journal
Carbohydr. Res. 338 (2003) 219-30.
  Sequence
[up:Q76FP5]
Reference
3  [PMID:14565843]
  Authors
Kotake T, Kaneko S, Kubomoto A, Haque MA, Kobayashi H, Tsumuraya Y.
  Title
Molecular cloning and expression in Escherichia coli of a Trichoderma viride endo-beta-(1-->6)-galactanase gene.
  Journal
Biochem. J. 377 (2004) 749-55.
  Sequence
[up:Q76FP5]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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