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Literature summary for 4.2.2.11 extracted from
- Molecular cloning, purification, and characterization of a novel polyMG-specific alginate lyase responsible for alginate MG block degradation in Stenotrophomas maltophilia KJ-2 (2012), Appl. Microbiol. Biotechnol., 95, 1643-1653.
Application
| Application | Comment | Organism |
|---|---|---|
| food industry | the KJ-2 polyMG-specific alginate lyase can be used in combination with other alginate lyases for a synergistic saccharification of alginate | Stenotrophomonas maltophilia |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Stenotrophomonas maltophilia |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | - |
Stenotrophomonas maltophilia |  |
| Cu2+ | - |
Stenotrophomonas maltophilia | |
| EDTA | - |
Stenotrophomonas maltophilia | |
| Hg2+ | - |
Stenotrophomonas maltophilia | |
| Mn2+ | - |
Stenotrophomonas maltophilia | |
| Zn2+ | - |
Stenotrophomonas maltophilia | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | required for activity, activates at 1 mM | Stenotrophomonas maltophilia | |
| K+ | activates at over 50 mM | Stenotrophomonas maltophilia | |
| Na+ | activates at over 50 mM | Stenotrophomonas maltophilia | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 47800 | - |
x * 47800, recombinant His-tagged enzyme, SDS-PAGE | Stenotrophomonas maltophilia |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Stenotrophomonas maltophilia | KJ-2 poly-mannuronate-guluronate-specific alginate lyase preferably degrades the glycosidic bond in beta-D-mannuronoyl-alpha-L-guluronate linkage than that in alpha-L-guluronoyl-beta-D-mannuronate linkage | ? | - |
? | |
| additional information | Stenotrophomonas maltophilia KJ-2 | KJ-2 poly-mannuronate-guluronate-specific alginate lyase preferably degrades the glycosidic bond in beta-D-mannuronoyl-alpha-L-guluronate linkage than that in alpha-L-guluronoyl-beta-D-mannuronate linkage | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Stenotrophomonas maltophilia | I6P4V6 | - |
- |
| Stenotrophomonas maltophilia KJ-2 | I6P4V6 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme by nickel affinity chromatography from Escherichia coli strain BL21(DE3) | Stenotrophomonas maltophilia |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | KJ-2 poly-mannuronate-guluronate-specific alginate lyase preferably degrades the glycosidic bond in beta-D-mannuronoyl-alpha-L-guluronate linkage than that in alpha-L-guluronoyl-beta-D-mannuronate linkage | Stenotrophomonas maltophilia | ? | - |
? | |
| additional information | alginate, poly-mannuronate-, poly-guluronate-, and poly-mannuronate-guluronate-block substrates are used, substrate specificity, cf. EC 4.2.2.3, overview. No or poor activity with chondroitin B, agarose, agar, starch, and pectin | Stenotrophomonas maltophilia | ? | - |
? | |
| additional information | KJ-2 poly-mannuronate-guluronate-specific alginate lyase preferably degrades the glycosidic bond in beta-D-mannuronoyl-alpha-L-guluronate linkage than that in alpha-L-guluronoyl-beta-D-mannuronate linkage | Stenotrophomonas maltophilia KJ-2 | ? | - |
? | |
| additional information | alginate, poly-mannuronate-, poly-guluronate-, and poly-mannuronate-guluronate-block substrates are used, substrate specificity, cf. EC 4.2.2.3, overview. No or poor activity with chondroitin B, agarose, agar, starch, and pectin | Stenotrophomonas maltophilia KJ-2 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 47800, recombinant His-tagged enzyme, SDS-PAGE | Stenotrophomonas maltophilia |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| alginate lyase | - |
Stenotrophomonas maltophilia |
| KJ-2 alginate lyase | - |
Stenotrophomonas maltophilia |
| polyMG-specific alginate lyase | - |
Stenotrophomonas maltophilia |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
- |
Stenotrophomonas maltophilia |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
purified recombinant His-tagged enzyme, 20 min, stable up to, significant loss of activity above | Stenotrophomonas maltophilia |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
- |
Stenotrophomonas maltophilia |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 8 | 9 | the purified recombinant His-tagged enzyme exhibits stable and high activity at pH between 8.0 and 9.0 | Stenotrophomonas maltophilia |
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