Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis

The coproporphyrin dependent heme biosynthesis pathway is almost exclusively utilized by Gram-positive bacteria. This fact makes it a worthwhile topic for basic research, since a fundamental understanding of a metabolic pathway is necessary to translate the focus towards medical biotechnology, which...

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Main Authors: Nikolaus Falb, Gaurav Patil, Paul G. Furtmüller, Thomas Gabler, Stefan Hofbauer
Format: Article
Language:English
Published: Elsevier 2023-01-01
Series:Computational and Structural Biotechnology Journal
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S2001037023002611
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author Nikolaus Falb
Gaurav Patil
Paul G. Furtmüller
Thomas Gabler
Stefan Hofbauer
author_facet Nikolaus Falb
Gaurav Patil
Paul G. Furtmüller
Thomas Gabler
Stefan Hofbauer
author_sort Nikolaus Falb
collection DOAJ
description The coproporphyrin dependent heme biosynthesis pathway is almost exclusively utilized by Gram-positive bacteria. This fact makes it a worthwhile topic for basic research, since a fundamental understanding of a metabolic pathway is necessary to translate the focus towards medical biotechnology, which is very relevant in this specific case, considering the need for new antibiotic targets to counteract the pathogenicity of Gram-positive superbugs. Over the years a lot of structural data on the set of enzymes acting in Gram-positive heme biosynthesis has accumulated in the Protein Database (www.pdb.org). One major challenge is to filter and analyze all available structural information in sufficient detail in order to be helpful and to draw conclusions. Here we pursued to give a holistic overview of structural information on enzymes involved in the coproporphyrin dependent heme biosynthesis pathway. There are many aspects to be extracted from experimentally determined structures regarding the reaction mechanisms, where the smallest variation of the position of an amino acid residue might be important, but also on a larger level regarding protein-protein interactions, where the focus has to be on surface characteristics and subunit (secondary) structural elements and oligomerization. This review delivers a status quo, highlights still missing information, and formulates future research endeavors in order to better understand prokaryotic heme biosynthesis.
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spelling doaj.art-ab02ec0ce2e047a6802aaf72e316ed4f2023-12-21T07:31:51ZengElsevierComputational and Structural Biotechnology Journal2001-03702023-01-012139333945Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesisNikolaus Falb0Gaurav Patil1Paul G. Furtmüller2Thomas Gabler3Stefan Hofbauer4University of Natural Resources and Life Sciences, Vienna, Department of Chemistry, Institute of Biochemistry, Muthgasse 18, A-1190 Vienna, AustriaUniversity of Natural Resources and Life Sciences, Vienna, Department of Chemistry, Institute of Biochemistry, Muthgasse 18, A-1190 Vienna, AustriaUniversity of Natural Resources and Life Sciences, Vienna, Department of Chemistry, Institute of Biochemistry, Muthgasse 18, A-1190 Vienna, AustriaUniversity of Natural Resources and Life Sciences, Vienna, Department of Chemistry, Institute of Biochemistry, Muthgasse 18, A-1190 Vienna, AustriaCorresponding author.; University of Natural Resources and Life Sciences, Vienna, Department of Chemistry, Institute of Biochemistry, Muthgasse 18, A-1190 Vienna, AustriaThe coproporphyrin dependent heme biosynthesis pathway is almost exclusively utilized by Gram-positive bacteria. This fact makes it a worthwhile topic for basic research, since a fundamental understanding of a metabolic pathway is necessary to translate the focus towards medical biotechnology, which is very relevant in this specific case, considering the need for new antibiotic targets to counteract the pathogenicity of Gram-positive superbugs. Over the years a lot of structural data on the set of enzymes acting in Gram-positive heme biosynthesis has accumulated in the Protein Database (www.pdb.org). One major challenge is to filter and analyze all available structural information in sufficient detail in order to be helpful and to draw conclusions. Here we pursued to give a holistic overview of structural information on enzymes involved in the coproporphyrin dependent heme biosynthesis pathway. There are many aspects to be extracted from experimentally determined structures regarding the reaction mechanisms, where the smallest variation of the position of an amino acid residue might be important, but also on a larger level regarding protein-protein interactions, where the focus has to be on surface characteristics and subunit (secondary) structural elements and oligomerization. This review delivers a status quo, highlights still missing information, and formulates future research endeavors in order to better understand prokaryotic heme biosynthesis.http://www.sciencedirect.com/science/article/pii/S2001037023002611Coproporphyrin ferrochelataseCoproheme decarboxylaseFrataxinCoproporphyrinogen oxidaseUroporphyrinogen decarboxylaseStructure determination
spellingShingle Nikolaus Falb
Gaurav Patil
Paul G. Furtmüller
Thomas Gabler
Stefan Hofbauer
Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis
Computational and Structural Biotechnology Journal
Coproporphyrin ferrochelatase
Coproheme decarboxylase
Frataxin
Coproporphyrinogen oxidase
Uroporphyrinogen decarboxylase
Structure determination
title Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis
title_full Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis
title_fullStr Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis
title_full_unstemmed Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis
title_short Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis
title_sort structural aspects of enzymes involved in prokaryotic gram positive heme biosynthesis
topic Coproporphyrin ferrochelatase
Coproheme decarboxylase
Frataxin
Coproporphyrinogen oxidase
Uroporphyrinogen decarboxylase
Structure determination
url http://www.sciencedirect.com/science/article/pii/S2001037023002611
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