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Literature summary extracted from
- An exo-beta-(1->3)-D-galactanase from Streptomyces sp. provides insights into type II arabinogalactan structure (2012), Carbohydr. Res., 352, 70-81.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.2.1.145 | analysis | the activity of the enzyme is well suited for the study of type II galactan structures and provides an important tool for the investigation of the biological role of arabinogalactan proteins in plants | Streptomyces sp. |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.145 | SGalase1, DNA and amino acid equence determination and analysis, sequence comparison, phylogenetic analysis and tree | Streptomyces sp. |
| 3.2.1.145 | SGalase2, DNA and amino acid equence determination and analysis, sequence comparison, phylogenetic analysis and tree | Streptomyces sp. |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.145 | 45000 | - |
x * 45000, about, SDS-PAGE, x * 48200, about, sequence calculation | Streptomyces sp. |
| 3.2.1.145 | 47900 | - |
x * 47900, about, sequence calculation | Streptomyces sp. |
| 3.2.1.145 | 48200 | - |
x * 45000, about, SDS-PAGE, x * 48200, about, sequence calculation | Streptomyces sp. |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.145 | additional information | Streptomyces sp. | the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins | ? | - |
? |  |
| 3.2.1.145 | additional information | Streptomyces sp. 19(2012) | the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.145 | Streptomyces sp. | I0B0S9 | SGalase1; isolated from culture filtrates of soil | - |
| 3.2.1.145 | Streptomyces sp. | I0B0T0 | SGalase2; isolated from culture filtrates of soil | - |
| 3.2.1.145 | Streptomyces sp. 19(2012) | I0B0S9 | SGalase1; isolated from culture filtrates of soil | - |
| 3.2.1.145 | Streptomyces sp. 19(2012) | I0B0T0 | SGalase2; isolated from culture filtrates of soil | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.145 | native enzyme 1.8fold from culture supernatant by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration | Streptomyces sp. |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.145 | 40 | - |
purified native enzyme, pH 3.8, 48°C | Streptomyces sp. |
| 3.2.1.145 | 40 | - |
purified native enzyme, pH 5.0, 48°C | Streptomyces sp. |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.145 | dearabinosylated gum arabic + H2O | de-arabinosylated gum arabic is used as a model to investigate the use of the enzyme in defining type II galactan structure, kinetics, overview. Exhaustive hydrolysis of dearabinosylated gum arabic resultes in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating, mass spectrometric analysis | Streptomyces sp. | ? | - |
? | |
| 3.2.1.145 | dearabinosylated gum arabic + H2O | de-arabinosylated gum arabic is used as a model to investigate the use of the enzyme in defining type II galactan structure, kinetics, overview. Exhaustive hydrolysis of dearabinosylated gum arabic resultes in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating., mass spectrometric analysis | Streptomyces sp. | ? | - |
? | |
| 3.2.1.145 | dearabinosylated gum arabic + H2O | de-arabinosylated gum arabic is used as a model to investigate the use of the enzyme in defining type II galactan structure, kinetics, overview. Exhaustive hydrolysis of dearabinosylated gum arabic resultes in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating., mass spectrometric analysis | Streptomyces sp. 19(2012) | ? | - |
? | |
| 3.2.1.145 | dearabinosylated gum arabic + H2O | de-arabinosylated gum arabic is used as a model to investigate the use of the enzyme in defining type II galactan structure, kinetics, overview. Exhaustive hydrolysis of dearabinosylated gum arabic resultes in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating, mass spectrometric analysis | Streptomyces sp. 19(2012) | ? | - |
? | |
| 3.2.1.145 | additional information | the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins | Streptomyces sp. | ? | - |
? | |
| 3.2.1.145 | additional information | the enzyme specifically hydrolyses beta-(1->3)-D-galacto-oligo- or poly-saccharides from the upstream (non-reducing) end, typical of an exo-acting enzyme. Substrate specificity, overview. No or negligible activity on 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-fucopyranoside,4-nitrophenyl alpha-L-arabinofuranosidase 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha/beta-D-glucopyranoside, 4-nitrophenyl alpha/beta-L-fucopyranoside, 4-nitrophenyl beta-D-cellobioside, 4-nitrophenyl alpha-D-mannopyranoside, or 4-nitrophenyl beta-D-xylopyranoside | Streptomyces sp. | ? | - |
? | |
| 3.2.1.145 | additional information | the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins | Streptomyces sp. 19(2012) | ? | - |
? | |
| 3.2.1.145 | additional information | the enzyme specifically hydrolyses beta-(1->3)-D-galacto-oligo- or poly-saccharides from the upstream (non-reducing) end, typical of an exo-acting enzyme. Substrate specificity, overview. No or negligible activity on 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-fucopyranoside,4-nitrophenyl alpha-L-arabinofuranosidase 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha/beta-D-glucopyranoside, 4-nitrophenyl alpha/beta-L-fucopyranoside, 4-nitrophenyl beta-D-cellobioside, 4-nitrophenyl alpha-D-mannopyranoside, or 4-nitrophenyl beta-D-xylopyranoside | Streptomyces sp. 19(2012) | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.145 | ? | x * 45000, about, SDS-PAGE, x * 48200, about, sequence calculation | Streptomyces sp. |
| 3.2.1.145 | ? | x * 47900, about, sequence calculation | Streptomyces sp. |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.145 | exo-beta-(1->3)-D-galactanase | - |
Streptomyces sp. |
| 3.2.1.145 | SGalase1 | - |
Streptomyces sp. |
| 3.2.1.145 | SGalase2 | - |
Streptomyces sp. |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.145 | 48 | - |
- |
Streptomyces sp. |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.145 | 3.8 | - |
- |
Streptomyces sp. |
| 3.2.1.145 | 5 | - |
- |
Streptomyces sp. |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 3.2.1.145 | Streptomyces sp. | about, sequence calculation | - |
7.45 |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.2.1.145 | evolution | the enzyme belongs to the glycoside hydrolase family 43, GH43, phylogenetic analysis and tree | Streptomyces sp. |
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