Title : Recombinant Arthromyces ramosus Peroxidase Has Similar Substrate Specificity Profiles as, but a Catalytic Efficiency up to 11-Fold Higher than, Horseradish Peroxidase.

Pub. Date : 2022 Jan 19

PMID : 34981926






3 Functional Relationships(s)
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1 In this work, rARP expressed by Komagataella phaffii had a production yield of 6.2 mg/L, up to 155-fold higher than ARP and other recombinant peroxidases, and a specific activity of 3240 units/mg toward 2,2"-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), up to 29-fold higher than HRP and other peroxidases. 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid kidney androgen regulated protein Rattus norvegicus
2 In this work, rARP expressed by Komagataella phaffii had a production yield of 6.2 mg/L, up to 155-fold higher than ARP and other recombinant peroxidases, and a specific activity of 3240 units/mg toward 2,2"-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), up to 29-fold higher than HRP and other peroxidases. 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid kidney androgen regulated protein Rattus norvegicus
3 The Michaelis constant (Km) and first-order rate constant (kcat) of rARP showed 10-fold substrate affinity and consequently 6-fold catalytic efficiency of HRP toward ABTS. 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid kidney androgen regulated protein Rattus norvegicus