In Vitro Assembly of Catalase.
(2014) In Journal of Biological Chemistry 289(41). p.28411-28420- Abstract
- Most aerobic organisms contain catalase which functions to decompose hydrogen peroxide. Typical catalases are structurally complex homo-tetrameric enzymes with one heme prosthetic group buried in each subunit. It is not known how catalase in the cell is assembled from its constituents. The bacterium Enterococcus faecalis cannot synthesize heme but can acquire it from the environment to form a cytoplasmic catalase. We have in E. faecalis monitored production of the enzyme polypeptide (KatA) depending on the availability of heme and used our findings to devise a procedure for the purification of preparative amounts of in vivo-synthesized apocatalase. We show that fully active catalase can be obtained in vitro by incubating isolated... (More)
- Most aerobic organisms contain catalase which functions to decompose hydrogen peroxide. Typical catalases are structurally complex homo-tetrameric enzymes with one heme prosthetic group buried in each subunit. It is not known how catalase in the cell is assembled from its constituents. The bacterium Enterococcus faecalis cannot synthesize heme but can acquire it from the environment to form a cytoplasmic catalase. We have in E. faecalis monitored production of the enzyme polypeptide (KatA) depending on the availability of heme and used our findings to devise a procedure for the purification of preparative amounts of in vivo-synthesized apocatalase. We show that fully active catalase can be obtained in vitro by incubating isolated apoprotein with hemin. We have characterized features of the assembly process and describe a temperature-trapped hemylated intermediate of the enzyme maturation process. Hemylation of apocatalase does not require auxiliary cell components but rapid assembly of active enzyme seemingly is assisted in the cell. Our findings provide insight about catalase assembly and offer new experimental possibilities for detailed studies of this process. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4614160
- author
- Baureder, Michael LU ; Barane, Elisabeth LU and Hederstedt, Lars LU
- organization
- publishing date
- 2014
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 289
- issue
- 41
- pages
- 28411 - 28420
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:25148685
- wos:000343765400034
- scopus:84907821989
- pmid:25148685
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M114.596148
- language
- English
- LU publication?
- yes
- id
- 498ff559-0c9e-41ae-b698-da05b610e657 (old id 4614160)
- date added to LUP
- 2016-04-01 10:13:23
- date last changed
- 2022-04-12 03:07:29
@article{498ff559-0c9e-41ae-b698-da05b610e657,
abstract = {{Most aerobic organisms contain catalase which functions to decompose hydrogen peroxide. Typical catalases are structurally complex homo-tetrameric enzymes with one heme prosthetic group buried in each subunit. It is not known how catalase in the cell is assembled from its constituents. The bacterium Enterococcus faecalis cannot synthesize heme but can acquire it from the environment to form a cytoplasmic catalase. We have in E. faecalis monitored production of the enzyme polypeptide (KatA) depending on the availability of heme and used our findings to devise a procedure for the purification of preparative amounts of in vivo-synthesized apocatalase. We show that fully active catalase can be obtained in vitro by incubating isolated apoprotein with hemin. We have characterized features of the assembly process and describe a temperature-trapped hemylated intermediate of the enzyme maturation process. Hemylation of apocatalase does not require auxiliary cell components but rapid assembly of active enzyme seemingly is assisted in the cell. Our findings provide insight about catalase assembly and offer new experimental possibilities for detailed studies of this process.}},
author = {{Baureder, Michael and Barane, Elisabeth and Hederstedt, Lars}},
issn = {{1083-351X}},
language = {{eng}},
number = {{41}},
pages = {{28411--28420}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{In Vitro Assembly of Catalase.}},
url = {{http://dx.doi.org/10.1074/jbc.M114.596148}},
doi = {{10.1074/jbc.M114.596148}},
volume = {{289}},
year = {{2014}},
}