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Literature summary for 4.1.2.10 extracted from

  • Pavkov-Keller, T.; Bakhuis, J.; Steinkellner, G.; Jolink, F.; Keijmel, E.; Birner-Gruenberger, R.; Gruber, K.
    Structures of almond hydroxynitrile lyase isoenzyme 5 provide a rationale for the lack of oxidoreductase activity in flavin dependent HNLs (2016), J. Biotechnol., 235, 24-31 .
    View publication on PubMed
Search for more literature for 4.1.2.10

Cloned(Commentary)

Cloned (Comment) Organism
mutant V317A of hydroxynitrile lyase isoenzyme 5 is expressed in Aspergillus niger Prunus dulcis
the highly glycosylated Prunus amygdalus HNL isoenzyme 5 (PaHNL5 V317A) is expressed in Aspergillus niger. The recombinant protein is highly glycosylated as confirmed by SDS-page and mass spectrometry Prunus dulcis

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structuture of mutant V317A of hydroxynitrile lyase isoenzyme 5 in complex with benzyl alcohol. The structure of is determined at a resolutionof 2.3 A by molecular replacement Prunus dulcis
vapor diffusion method, high resolution X-ray structure of the highly glycosylated Prunus amygdalus HNL isoenzyme 5 (PaHNL5 V317A) expressed in Aspergillus niger and its complex with benzyl alcohol. In PaHNLs benzyl alcohol is bound too far away from the FAD cofactor in order to be oxidized Prunus dulcis

Organism

Organism UniProt Comment Textmining
Prunus dulcis O24243
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
 Prunus dulcis
glycoprotein the mass difference between the glycosylated and deglycosylated form of the recombinant protein expressed in Aspergillus niger averages to 25 kDa, which indicates that more than one sugar unit is attached to the glycosylated Asn residues Prunus dulcis

Purification (Commentary)

Purification (Comment) Organism
-
 Prunus dulcis
mutant enzyme V317A Prunus dulcis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
 in the pH-range 4-8 the Tm is constant at 76°C. At pH 9 and 10 the Tm values are slightly lower, 70°C and the lowest Tm of 65°C is measured at pH 3 Prunus dulcis
65
-
 Tm-value at pH 3 Prunus dulcis
70
-
 in the pH-range 4-8 the Tm is constant at 76°C. At pH 9 and 10 the Tm values are slightly lower, 70°C and the lowest Tm of 65°C is measured at pH 3 Prunus dulcis
70
-
 Tm-value at pH 9 and 10 Prunus dulcis
76
-
 in the pH-range 4-8 the Tm is constant at 76°C. At pH 9 and 10 the Tm values are slightly lower, 70°C and the lowest Tm of 65°C is measured at pH 3 Prunus dulcis
76
-
 Tm-value in the pH-range 4-8 Prunus dulcis

Cofactor

Cofactor Comment Organism Structure
FAD benzyl alcohol is bound too far away from the FAD cofactor in order to be oxidized Prunus dulcis
FAD thee structure of PaHNL5 in complex with benzyl alcohol shows that this compound binds too far away from the FAD cofactor in order to directly participate in the redox mechanism proposed for aryl-alcohol oxidases Prunus dulcis

General Information

General Information Comment Organism
metabolism the enzyme is involved in a process called cyanogenesis. They possess an important biological role in plant defense against herbivoral and fungal attack due to the bitter taste and the release of toxic hydrogen cyanide upon tissue disruption Prunus dulcis
physiological function the enzyme is involved in aprocess called cyanogenesis. They possess an important biological role in plant defense against herbivoral and fungal attack due to the bitter taste and the release of toxic hydrogen cyanide upon tissue disruption Prunus dulcis