Cloned (Comment) | Organism |
---|---|
recombinant expression in Escherichia coli | Aspergillus niger |
recombinant expression in Escherichia coli | Lipomyces starkeyi |
Protein Variants | Comment | Organism |
---|---|---|
additional information | LGK derived from Lipomyces starkeyi is an interesting target for efforts in advanced protein engineering, single-site saturation mutagenesis coupled with selection of the LGK variants using deep sequencing approaches is used to develop LGK constructs with enhanced thermal stability and catalytic efficiency | Lipomyces starkeyi |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ADP | - |
Aspergillus niger | |
gentiobiose | a non-competitive inhibitor | Sporidiobolus salmonicolor | |
Mg-ADP | competitive inhibition | Sporidiobolus salmonicolor | |
Tris | - |
Lipomyces starkeyi |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.19 | - |
ATP | pH and temperature not specified in the publication | Sporidiobolus salmonicolor | |
0.2 | 0.68 | ATP | pH 9.0, 30°C | Lipomyces starkeyi | |
0.21 | - |
ATP | pH and temperature not specified in the publication | Penicillium herquei | |
0.25 | - |
ATP | pH 9.3, 30°C | Aspergillus niger | |
0.29 | - |
ATP | pH and temperature not specified in the publication | Penicillium javanicum | |
0.29 | - |
ATP | pH and temperature not specified in the publication | Papiliotrema flavescens | |
0.3 | - |
ATP | pH and temperature not specified in the publication | Papiliotrema laurentii | |
0.3 | - |
ATP | pH and temperature not specified in the publication | Alternaria alternata | |
0.3 | - |
ATP | pH and temperature not specified in the publication | Buckleyzyma aurantiaca | |
0.35 | - |
ATP | pH and temperature not specified in the publication | Hannaella luteola | |
48 | - |
1,6-anhydro-beta-D-glucopyranose | pH and temperature not specified in the publication | Penicillium herquei | |
56 | - |
1,6-anhydro-beta-D-glucopyranose | pH and temperature not specified in the publication | Penicillium javanicum | |
60 | - |
1,6-anhydro-beta-D-glucopyranose | pH 9.3, 30°C | Aspergillus niger | |
68.6 | 105.3 | 1,6-anhydro-beta-D-glucopyranose | pH 9.0, 30°C | Lipomyces starkeyi | |
70 | - |
1,6-anhydro-beta-D-glucopyranose | pH and temperature not specified in the publication | Alternaria alternata | |
71.2 | - |
1,6-anhydro-beta-D-glucopyranose | pH 9.3, 30°C | Aspergillus niger | |
80 | - |
1,6-anhydro-beta-D-glucopyranose | pH and temperature not specified in the publication | Papiliotrema flavescens | |
84 | - |
1,6-anhydro-beta-D-glucopyranose | pH and temperature not specified in the publication | Papiliotrema laurentii | |
85 | - |
1,6-anhydro-beta-D-glucopyranose | pH and temperature not specified in the publication | Sporidiobolus salmonicolor | |
95 | - |
1,6-anhydro-beta-D-glucopyranose | pH and temperature not specified in the publication | Hannaella luteola | |
102 | - |
1,6-anhydro-beta-D-glucopyranose | pH and temperature not specified in the publication | Buckleyzyma aurantiaca | |
119 | - |
1,6-anhydro-beta-D-glucopyranose | pH and temperature not specified in the publication | Lipomyces starkeyi |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Aspergillus niger | |
Mg2+ | required | Sporidiobolus salmonicolor | |
Mg2+ | required | Aspergillus terreus | |
Mg2+ | required | Papiliotrema laurentii | |
Mg2+ | required | Penicillium javanicum | |
Mg2+ | required | Alternaria alternata | |
Mg2+ | required | Buckleyzyma aurantiaca | |
Mg2+ | required | Papiliotrema flavescens | |
Mg2+ | required | Penicillium herquei | |
Mg2+ | required | Hannaella luteola | |
Mg2+ | the enzyme requires Mg2+ or Mn2+, apparent binding of two magnesium ions in the active site showing ideal octahedral binding of the metals. The first of the bound metals, designated M1, forms an electrostatic interaction with the beta-phosphate, and its positioning suggests that it plays a direct role in phosphoryl transfer. The second of these metals, designated M2, likely plays a key role in coordinating the position of the alpha- and beta-phosphates since it binds to both of these phosphates, although a role in modulation of electrostatic charges is also plausible | Lipomyces starkeyi | |
Mn2+ | the enzyme requires Mg2+ or Mn2+, apparent binding of two magnesium ions in the active site showing ideal octahedral binding of the metals. The first of the bound metals, designated M1, forms an electrostatic interaction with the beta-phosphate, and its positioning suggests that it plays a direct role in phosphoryl transfer. The second of these metals, designated M2, likely plays a key role in coordinating the position of the alpha- and beta-phosphates since it binds to both of these phosphates, although a role in modulation of electrostatic charges is also plausible | Lipomyces starkeyi |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + levoglucosan + H2O | Aspergillus niger | - |
ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | Sporidiobolus salmonicolor | - |
ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | Aspergillus terreus | - |
ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | Papiliotrema laurentii | - |
ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | Penicillium javanicum | - |
ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | Alternaria alternata | - |
ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | Buckleyzyma aurantiaca | - |
ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | Papiliotrema flavescens | - |
ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | Lipomyces starkeyi | - |
ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | Penicillium herquei | - |
ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | Hannaella luteola | - |
ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | Aspergillus niger CBX-209 | - |
ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | Lipomyces starkeyi YZ-215 | - |
ADP + D-glucopyranose 6-phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Alternaria alternata | - |
- |
- |
Aspergillus niger | - |
- |
- |
Aspergillus niger CBX-209 | - |
- |
- |
Aspergillus terreus | - |
- |
- |
Buckleyzyma aurantiaca | - |
- |
- |
Hannaella luteola | - |
- |
- |
Lipomyces starkeyi | B3VI55 | - |
- |
Lipomyces starkeyi YZ-215 | B3VI55 | - |
- |
Papiliotrema flavescens | - |
- |
- |
Papiliotrema laurentii | - |
- |
- |
Penicillium herquei | - |
- |
- |
Penicillium javanicum | - |
- |
- |
Sporidiobolus salmonicolor | - |
- |
- |
Purification (Comment) | Organism |
---|---|
native enzyme by ion exchange chromatography | Sporidiobolus salmonicolor |
native enzyme by ion exchange chromatography | Aspergillus terreus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + 1,6-anhydro-beta-D-glucopyranose + H2O = ADP + 6-phospho-alpha-D-glucopyranose | the catalytic mechanism involves both cleavage of the 1,6-intramolecular linkage as well as phosphorylation | Sporidiobolus salmonicolor | |
ATP + 1,6-anhydro-beta-D-glucopyranose + H2O = ADP + 6-phospho-alpha-D-glucopyranose | the catalytic mechanism involves both cleavage of the 1,6-intramolecular linkage as well as phosphorylation | Aspergillus terreus |
Storage Stability | Organism |
---|---|
-20°C, recombinant enzyme, stable at | Aspergillus niger |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + levoglucosan + H2O | - |
Aspergillus niger | ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | - |
Sporidiobolus salmonicolor | ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | - |
Aspergillus terreus | ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | - |
Papiliotrema laurentii | ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | - |
Penicillium javanicum | ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | - |
Alternaria alternata | ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | - |
Buckleyzyma aurantiaca | ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | - |
Papiliotrema flavescens | ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | - |
Lipomyces starkeyi | ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | - |
Penicillium herquei | ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | - |
Hannaella luteola | ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | - |
Sporidiobolus salmonicolor | ADP + D-glucopyranose 6-phosphate | reaction products ADP and glucose 6-phosphate are measured by a pyruvatekinase/lactate dehydrogenase coupling system as well as through the use of 14C labeled levoglucosan and thin layer chromatography techniques | ? | |
ATP + levoglucosan + H2O | - |
Aspergillus terreus | ADP + D-glucopyranose 6-phosphate | reaction products ADP and glucose 6-phosphate are measured by a pyruvatekinase/lactate dehydrogenase coupling system as well as through the use of 14C labeled levoglucosan and thin layer chromatography techniques | ? | |
ATP + levoglucosan + H2O | structure-function analysis and reaction mechanism | Lipomyces starkeyi | ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | - |
Aspergillus niger CBX-209 | ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | - |
Lipomyces starkeyi YZ-215 | ADP + D-glucopyranose 6-phosphate | - |
? | |
ATP + levoglucosan + H2O | structure-function analysis and reaction mechanism | Lipomyces starkeyi YZ-215 | ADP + D-glucopyranose 6-phosphate | - |
? | |
additional information | enzme LGK shows specificity for the levoglucosan sugar, showing activity for only this anhydrosugar and no activity for galactosan or maltosan and only very weak activity for mannosan (1% relative activity) that also contain the same 1,6-anhydro intramolecular linkage as levoglucosan, demonstrating that the nature of the pyranose frame is also important for substrate recognition by enzyme LGK | Sporidiobolus salmonicolor | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
LGK | - |
Aspergillus niger |
LGK | - |
Sporidiobolus salmonicolor |
LGK | - |
Aspergillus terreus |
LGK | - |
Papiliotrema laurentii |
LGK | - |
Penicillium javanicum |
LGK | - |
Alternaria alternata |
LGK | - |
Buckleyzyma aurantiaca |
LGK | - |
Papiliotrema flavescens |
LGK | - |
Lipomyces starkeyi |
LGK | - |
Penicillium herquei |
LGK | - |
Hannaella luteola |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
- |
Aspergillus niger |
30 | - |
- |
Lipomyces starkeyi |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
5 | 30 | stable at, activity drops off sharply between 30°C and 40°C | Aspergillus niger |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9 | - |
- |
Lipomyces starkeyi |
9.3 | - |
- |
Aspergillus niger |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
6 | 10 | recombinant enzyme, stable at | Aspergillus niger |
7 | 10 | stable at | Aspergillus niger |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Aspergillus niger | |
ATP | - |
Sporidiobolus salmonicolor | |
ATP | - |
Aspergillus terreus | |
ATP | - |
Papiliotrema laurentii | |
ATP | - |
Penicillium javanicum | |
ATP | - |
Alternaria alternata | |
ATP | - |
Buckleyzyma aurantiaca | |
ATP | - |
Papiliotrema flavescens | |
ATP | - |
Lipomyces starkeyi | |
ATP | - |
Penicillium herquei | |
ATP | - |
Hannaella luteola |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
48 | - |
Tris | pH 9.0, 30°C | Lipomyces starkeyi |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.015 | - |
pH and temperature not specified in the publication | Sporidiobolus salmonicolor | Mg-ADP | |
0.05 | - |
pH and temperature not specified in the publication | Sporidiobolus salmonicolor | gentiobiose | |
0.2 | - |
pH 9.3, 30°C | Aspergillus niger | ADP |
General Information | Comment | Organism |
---|---|---|
additional information | three dimensional structure analysis, comparison of structure and mechanism with 1,6-anhydro-N-acetylmuramic acid kinase and AnmK-like enzymes, overview | Lipomyces starkeyi |