Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.1.232 extracted from

  • Bacik, J.P.; Jarboe, L.R.
    Bioconversion of anhydrosugars: emerging concepts and strategies (2016), IUBMB Life, 68, 700-708.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression in Escherichia coli Aspergillus niger
recombinant expression in Escherichia coli Lipomyces starkeyi

Protein Variants

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

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 [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

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/ Products (Substrates)

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

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 (Commentary)

Purification (Comment) Organism
native enzyme by ion exchange chromatography Sporidiobolus salmonicolor
native enzyme by ion exchange chromatography Aspergillus terreus

Reaction

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

Storage Stability Organism
-20°C, recombinant enzyme, stable at Aspergillus niger

Substrates and Products (Substrate)

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

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
Aspergillus niger
30
-
-
Lipomyces starkeyi

Temperature Stability [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
Lipomyces starkeyi
9.3
-
-
Aspergillus niger

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 10 recombinant enzyme, stable at Aspergillus niger
7 10 stable at Aspergillus niger

Cofactor

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 [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
48
-
Tris pH 9.0, 30°C Lipomyces starkeyi

IC50 Value

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

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