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. 2020 Jun 29;13:114. doi: 10.1186/s13068-020-01753-5

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© The Author(s) 2020

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 6 — Investigation of degron modification. Representative ADs from P. marinus (ADpm), N. punctiforme (ADnp) and S. elongatus (ADse). a-c Comparison of specific activities, enzyme abundance and pentane production in three representative ADs with and without degron. Enzyme abundance was normalized to ADpm based on peak area. d Comparison of enzyme abundance and pentane production in ADse C-terminal His-tag and N-terminal His-tag. e Modeling of protein–protein interaction between ADse and ferredoxin from E. coli. E. coli 2Fe2S ferredoxin (Uniprot ID P0A9R4) (colored pink) and ADse decarbonylase (colored wheat) interaction model predicted with GRAMMX protein–protein docking server. The C- and N-terminal ends of ADse are designated. f C-terminal His-tag effect on degron sealing. The data shows the mean of three replicates, and all error bars show the S.D