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

BRENDA support

Literature summary extracted from

  • Miyakawa, T.; Mizushima, H.; Ohtsuka, J.; Oda, M.; Kawai, F.; Tanokura, M.
    Structural basis for the Ca2+-enhanced thermostability and activity of PET-degrading cutinase-like enzyme from Saccharomonospora viridis AHK190 (2015), Appl. Microbiol. Biotechnol., 99, 4297-4307 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.74
-
 Saccharomonospora viridis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.74 crystal structures of S226P mutant in the Ca2+-bound and free states at 1.75 and 1.45 A resolution, respectively. A Ca2+ ion is coordinated by four residues within loop regions (the Ca2+ site) and two water molecules in a tetragonal bipyramidal array. The binding of Ca2+ induces large conformational changes in three loops, accompanied by the formation of additional interactions. The binding of Ca2+ stabilizes a region that is flexible in the Ca2+-free state but also modifies the substrate-binding groove by stabilizing an open conformation that allows the substrate to bind easily Saccharomonospora viridis

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.74 S226P mutant shows the highest activities toward tricaproin and tributyrin, the activity is greatly reduced toward tricaprylin Saccharomonospora viridis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.74 Ca2+ the binding of Ca2+ induces large conformational changes in three loops, accompanied by the formation of additional interactions. The binding of Ca2+ stabilizes a region that is flexible in the Ca2+-free state but also modifies the substrate-binding groove by stabilizing an open conformation that allows the substrate to bind easily Saccharomonospora viridis

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.74 Saccharomonospora viridis W0TJ64
-
-
3.1.1.74 Saccharomonospora viridis AHK190 W0TJ64
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.74 tributyrin + H2O about 85% of the activity with tricaproin, mutant S226P Saccharomonospora viridis butyric acid + 1,2-dibutyrylglycerol
-
 ?
3.1.1.74 tributyrin + H2O about 85% of the activity with tricaproin, mutant S226P Saccharomonospora viridis AHK190 butyric acid + 1,2-dibutyrylglycerol
-
 ?
3.1.1.74 tricaproin + H2O
-
 Saccharomonospora viridis ?
-
 ?
3.1.1.74 tricaproin + H2O
-
 Saccharomonospora viridis AHK190 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.74 Cut190
-
 Saccharomonospora viridis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.74 59
-
 melting temperature, mutant S226P Saccharomonospora viridis
3.1.1.74 73
-
 melting temperature, mutant S226P, presence of 100 mM Ca2+ Saccharomonospora viridis
3.1.1.74 75
-
 melting temperature, mutant S226P, presence of 300 mM Ca2+ Saccharomonospora viridis