Literature DB >> 2518519

Isolation and some properties of lysine N6-hydroxylase from Escherichia coli strain EN222.

H J Plattner1, P Pfefferle, A Romaguera, S Waschütza, H Diekmann.   

Abstract

Lysine N6-hydroxylase was isolated as a soluble enzyme from the supernatant after ultrasonication of Escherichia coli strain EN222 which contained the structural gene on a multicopy plasmid (as described by Engelbrecht and Braun in 1986). The apoenzyme prepared by dialysis was purified by ammonium sulfate precipitation and fast protein liquid chromatography using Superose 12 and Mono Q columns. The molecular mass as determined by gel filtration was 200 kDa and 50 kDa by SDS/polyacrylamide gel electrophoresis. The enzyme binds 0.79 molecule FAD/50 kDa. The activity of the enzyme is strictly dependent on NADPH. Its properties are similar to other flavoprotein monooxygenases of the EC group 1.14.13.

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Year:  1989        PMID： 2518519     DOI： 10.1007/bf01116193

Source DB:  PubMed          Journal:  Biol Met        ISSN： 0933-5854


  15 in total

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Review 3.  Microbial iron compounds.

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5.  Identification of the genes and their polypeptide products responsible for aerobactin synthesis by pColV plasmids.

Authors:  R Gross; F Engelbrecht; V Braun
Journal:  Mol Gen Genet       Date:  1985

6.  Effect of metabolites on epsilon-N-hydroxylysine formation in cell-free extracts of Aerobacter aerogenes 62-1.

Authors:  G J Murray; G E Clark; M A Parniak; T Viswanatha
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7.  Genetic and biochemical characterization of the aerobactin synthesis operon on pColV.

Authors:  R Gross; F Engelbrecht; V Braun
Journal:  Mol Gen Genet       Date:  1984

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Authors:  M Herrero; V de Lorenzo; J B Neilands
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9.  Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12.

Authors:  V de Lorenzo; A Bindereif; B H Paw; J B Neilands
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10.  Studies on the formation of N6-hydroxylysine in cell-free extracts of Aerobacter aerogenes 62-1.

Authors:  M A Parniak; G E Jackson; G J Murray; T Viswanatha
Journal:  Biochim Biophys Acta       Date:  1979-07-11
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5.  An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation.

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9.  Crystallographic evidence of drastic conformational changes in the active site of a flavin-dependent N-hydroxylase.

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  9 in total

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