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B6db references: 29694778

type Journal Article
authors Park YJ, Kenney GE, Schachner LF, Kelleher NL, Rosenzweig AC.
title Repurposed HisC Aminotransferases Complete the Biosynthesis of Some Methanobactins.
journal Biochemistry.
Activity mbnn
Family mbnn
PLP Fold Type 1
sel selected
ui 29694778
year (2018)
volume 57
number 25
pages 3515-3523
abstract Methanobactins (Mbns) are ribosomally produced, post-translationally modified bacterial natural products with a high affinity for copper. MbnN, a pyridoxal 5'-phosphate (PLP) dependent aminotransferase, performs a transamination reaction that is the last step in the biosynthesis of Mbns produced by several Methylosinus ( Ms.) species. Our bioinformatic analyses indicate that MbnNs likely derive from histidinol-phosphate aminotransferases (HisCs), which play a key role in histidine biosynthesis. A comparison of the HisC active site with the predicted MbnN structure suggests that MbnN's active site is altered to accommodate the larger and more hydrophobic substrates necessary for Mbn biosynthesis. Moreover, we have confirmed that MbnN is capable of catalyzing the final transamination step in Mbn biosynthesis in vitro and in vivo. We also demonstrate that without this final modification, Mbn would exhibit significantly decreased stability under physiological conditions. An examination of other Mbns and Mbn operons suggests that N-terminal protection of this family of natural products is of critical importance, and that several different means of N-terminal stabilization have evolved independently in Mbn subfamilies.

last changed 2018/10/19 13:15

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