The pro-enzyme C-terminal processing domain of Pholiota nameko tyrosinase is responsible for folding of the N-terminal catalytic domain
Gespeichert in:
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)
Online Zugang:
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| 008 | 210128e20150701xx s 000 0 eng | ||
| 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 | ||