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Literature summary for 3.2.1.23 extracted from

  • Shipkowski, S.; Brenchley, J.E.
    Bioinformatic, genetic, and biochemical evidence that some glycoside hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer hydrolases (2006), Appl. Environ. Microbiol., 72, 7730-7738.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
genes yesZ, lacA and galA, genetic organization, library construction and screening for 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside hydrolyzing activity, expression of His-tagged enzymes in Escherichia coli, cells expressing LacA with GalA gain the ability to use galactan as a carbon source Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
additional information construction of LacA and GalA knockout mutants, the increased beta-galactosidase activity generated in response to the addition of galactan is eliminated by inactivating lacA or galA but unaffected by the inactivation of yesZ, overview Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
Co2+ recombinant LacA Bacillus subtilis
Cu2+ recombinant LacA Bacillus subtilis
Zn2+ recombinant LacA Bacillus subtilis

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular GH53 enzyme GalA Bacillus subtilis
-
-
intracellular GH42 enzyme LacA Bacillus subtilis 5622
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
galactan + H2O Bacillus subtilis the GHF 42 enzyme LacA can act on the oligosaccharides released by the GH53 enzyme GalA from galactan, overview ?
-
?
galactotetraose + H2O Bacillus subtilis the GHF 42 enzyme LacA can act on the oligosaccharides released by the GH53 enzyme GalA from galactan, overview beta-D-galactose
-
?
additional information Bacillus subtilis regulation and physiologic functions of LacA and GalA, GH42 and GH53 enzymes, overview ?
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
genes yesZ, lacA and galA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged LacA from Escherichia coli by nickel affinity chromatography Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-nitrophenyl beta-D-galactopyranoside + H2O
-
Bacillus subtilis 2-nitrophenol + beta-D-galactose
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
-
Bacillus subtilis 4-nitrophenol + beta-D-galactose
-
?
5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside + H2O
-
Bacillus subtilis 5-bromo-4-chloroindol + beta-D-galactose
-
?
galactan + H2O the GHF 42 enzyme LacA can act on the oligosaccharides released by the GH53 enzyme GalA from galactan, overview Bacillus subtilis ?
-
?
galactotetraose + H2O the GHF 42 enzyme LacA can act on the oligosaccharides released by the GH53 enzyme GalA from galactan, overview Bacillus subtilis beta-D-galactose
-
?
additional information regulation and physiologic functions of LacA and GalA, GH42 and GH53 enzymes, overview Bacillus subtilis ?
-
?
additional information enzyme substrate specificity, overview Bacillus subtilis ?
-
?

Synonyms

Synonyms Comment Organism
GALA
-
Bacillus subtilis
galactanase
-
Bacillus subtilis
LacA
-
Bacillus subtilis
More the enzymes LacAand YesZ, and GalA belong to the glycosyl hydrolase families 42 and 43, respectively Bacillus subtilis
YesZ
-
Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
recombinant LacA Bacillus subtilis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
40 60
-
Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
purified recombinant LacA, stable up to Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 6.5 recombinant LacA Bacillus subtilis