The pro-enzyme C-terminal processing domain of Pholiota nameko tyrosinase is responsible for folding of the N-terminal catalytic domain

Verfasser / Beitragende:
[Lai Moe, Saya Maekawa, Yasuko Kawamura-Konishi]
Ort, Verlag, Jahr:
2015
Enthalten in:
Applied Microbiology and Biotechnology, 99/13(2015-07-01), 5499-5510
Format:
Artikel (online)
ID: 605506124
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024 7 0 |a 10.1007/s00253-015-6597-y  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00253-015-6597-y 
245 0 4 |a The pro-enzyme C-terminal processing domain of Pholiota nameko tyrosinase is responsible for folding of the N-terminal catalytic domain  |h [Elektronische Daten]  |c [Lai Moe, Saya Maekawa, Yasuko Kawamura-Konishi] 
520 3 |a Pholiota nameko (Pholiota microspore) tyrosinase is expressed as a latent 67-kDa pro-tyrosinase, comprising a 42-kDa N-terminal catalytic domain with a binuclear copper centre and a 25-kDa C-terminal domain and is activated by proteolytic digestion of the C-terminal domain. To investigate the role of the C-terminal processing domain of pro-tyrosinase, we constructed a recombinant tyrosinase lacking the C-terminal domain and four recombinant pro-tyrosinase mutants (F515G, H539N, L540G and Y543G) carrying substituted amino acid residues on the C-terminal domain. The recombinant tyrosinase lacking the C-terminal domain had no catalytic activity; whereas the mutant L540G was copper depleted, the other mutants had copper contents similar to that of the wild-type pro-tyrosinase. Proteolytic digestion activated the mutants H539N and Y543G following release of the C-terminal domain, and the resulting tyrosinases had higher K m values for t-butyl catechol than the wild-type pro-tyrosinase. The mutants F515G and L540G were degraded by proteolytic digestion and yielded smaller proteins with no activity. These data suggest that the C-terminal processing domain of P. nameko pro-tyrosinase is essential for correct folding of the N-terminal catalytic domain and acts as an intramolecular chaperone during assembly of the active-site conformation. 
540 |a Springer-Verlag Berlin Heidelberg, 2015 
690 7 |a Pholiota nameko  |2 nationallicence 
690 7 |a Tyrosinase  |2 nationallicence 
690 7 |a Pro-enzyme  |2 nationallicence 
690 7 |a Processing  |2 nationallicence 
690 7 |a Chaperone  |2 nationallicence 
700 1 |a Moe  |D Lai  |u Department of Food Science, Faculty of Bioresources and Environmental Sciences, Ishikawa Prefectural University, 1-308 Suematsu, 921-8836, Nonoichi, Ishikawa, Japan  |4 aut 
700 1 |a Maekawa  |D Saya  |u Department of Food Science, Faculty of Bioresources and Environmental Sciences, Ishikawa Prefectural University, 1-308 Suematsu, 921-8836, Nonoichi, Ishikawa, Japan  |4 aut 
700 1 |a Kawamura-Konishi  |D Yasuko  |u Department of Food Science, Faculty of Bioresources and Environmental Sciences, Ishikawa Prefectural University, 1-308 Suematsu, 921-8836, Nonoichi, Ishikawa, Japan  |4 aut 
773 0 |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/13(2015-07-01), 5499-5510  |x 0175-7598  |q 99:13<5499  |1 2015  |2 99  |o 253 
856 4 0 |u https://doi.org/10.1007/s00253-015-6597-y  |q text/html  |z Onlinezugriff via DOI 
898 |a BK010053  |b XK010053  |c XK010000 
900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a research-article  |2 jats 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-springer 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1007/s00253-015-6597-y  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Moe  |D Lai  |u Department of Food Science, Faculty of Bioresources and Environmental Sciences, Ishikawa Prefectural University, 1-308 Suematsu, 921-8836, Nonoichi, Ishikawa, Japan  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Maekawa  |D Saya  |u Department of Food Science, Faculty of Bioresources and Environmental Sciences, Ishikawa Prefectural University, 1-308 Suematsu, 921-8836, Nonoichi, Ishikawa, Japan  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Kawamura-Konishi  |D Yasuko  |u Department of Food Science, Faculty of Bioresources and Environmental Sciences, Ishikawa Prefectural University, 1-308 Suematsu, 921-8836, Nonoichi, Ishikawa, Japan  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/13(2015-07-01), 5499-5510  |x 0175-7598  |q 99:13<5499  |1 2015  |2 99  |o 253