Enzymes in Recombinant Proteins

Protocatechuate 3,4-dioxygenase is a bacterial enzyme, which is sourced from Pseudomonas sp. This enzyme operates by catalyzing the cleavage of aromatic rings in protocatechuate, a derivative of catechol. Its mode of action involves the incorporation of oxygen into protocatechuate, resulting in the formation of beta-carboxy-cis,cis-muconate. This reaction is crucial for the microbial degradation of aromatic compounds, thereby playing a significant role in the biodegradation pathways of lignin-derived aromatic pollutants.

Alteplase is human plasminogen activator (EC 3.4.21.68, that cleaves plasminogen into enzymatically active form, plasmin), recombinantly expressed in CHO cells. Alteplase belongs to the group of thrombolytic agents, and it has shown to be effective in restoring blood flow by breaking down clots.

Glucosyltransferase (GTase) is the enzyme that transfers glucose to another organic molecule (aglycon), establishing glycosidic linkage. UDP-glucose dependent GTases are part of the enzyme family of glucosyltransferases, they are versatile tools in glucosylation reactions. Different GTases have different substrate specificities. For the specificity of GT205 Glucosyltransferase, please see Table 1 that lists the available GTases with GT205 highlighted.Color: beigeForm: lyophilisateProtein content: 0.5 mg/mgThe glucosyltransferase was tested in a glucosylation reaction of a preferred substrate. High conversion after up to 24 hr reaction time was observed.
Not sure which GTase to choose? Consider our Glucosyltransferase kit, which contains all 8 Glucosyltransferases.