MioC is an FMN-binding protein that is essential for Escherichia coli biotin synthase activity in vitro
MioC is an FMN-binding protein that is essential for Escherichia coli biotin synthase activity in vitro
Biotin synthase is required for the conversion of dethiobiotin to biotin and requires a number of accessory proteins and small molecule cofactors for activity in vitro. We have previously identified two of these proteins as flavodoxin and ferredoxin (flavodoxin) NADP(+) reductase. We now report the identification of MioC as a third essential protein, together with its cloning, purification, and characterization. Purified MioC has a UV-visible spectrum characteristic of a flavoprotein and contains flavin mononucleotide. The presence of flavin mononucleotide and the primary sequence similarity to flavodoxin suggest that. MioC may function as an electron transport protein. The role of MioC in the biotin synthase reaction is discussed, and the structure and function of MioC is compared with that of flavodoxin.
s-adenosylmethionine, gene-cluster, replication, flavodoxin, transcription, dethiobiotin, mechanism, sequence, sulfur, initiation
32277-32280
Birch, O. M.
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Hewitson, K. S.
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Fuhrmann, M.
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Burgdorf, K.
d39b5b0f-d8a2-401f-8ef9-0ba57933ff15
Baldwin, J. E.
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Roach, P. L.
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Shaw, N. M.
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13 October 2000
Birch, O. M.
70f322ee-99ae-46d1-a45f-02cd23511350
Hewitson, K. S.
80aed1e5-55db-4e5f-9d56-da42548e4d00
Fuhrmann, M.
f763a6cc-7c3a-4874-8a16-6a2b3c829453
Burgdorf, K.
d39b5b0f-d8a2-401f-8ef9-0ba57933ff15
Baldwin, J. E.
0a1a3673-4e83-4409-9bc4-dbb67832085d
Roach, P. L.
41af1c64-d925-472f-af2b-63e8a2eb342b
Shaw, N. M.
5b71a351-cade-44b6-9301-633c65cdcbb6
Birch, O. M., Hewitson, K. S., Fuhrmann, M., Burgdorf, K., Baldwin, J. E., Roach, P. L. and Shaw, N. M.
(2000)
MioC is an FMN-binding protein that is essential for Escherichia coli biotin synthase activity in vitro.
The Journal of Biological Chemistry, 275 (41), .
(doi:10.1074/jbc.M004497200).
Abstract
Biotin synthase is required for the conversion of dethiobiotin to biotin and requires a number of accessory proteins and small molecule cofactors for activity in vitro. We have previously identified two of these proteins as flavodoxin and ferredoxin (flavodoxin) NADP(+) reductase. We now report the identification of MioC as a third essential protein, together with its cloning, purification, and characterization. Purified MioC has a UV-visible spectrum characteristic of a flavoprotein and contains flavin mononucleotide. The presence of flavin mononucleotide and the primary sequence similarity to flavodoxin suggest that. MioC may function as an electron transport protein. The role of MioC in the biotin synthase reaction is discussed, and the structure and function of MioC is compared with that of flavodoxin.
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Published date: 13 October 2000
Keywords:
s-adenosylmethionine, gene-cluster, replication, flavodoxin, transcription, dethiobiotin, mechanism, sequence, sulfur, initiation
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Local EPrints ID: 18971
URI: http://eprints.soton.ac.uk/id/eprint/18971
ISSN: 0021-9258
PURE UUID: fcd7d874-c56b-4c1c-b470-6a819858605a
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Date deposited: 19 Jan 2006
Last modified: 15 Mar 2024 06:09
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Author:
O. M. Birch
Author:
K. S. Hewitson
Author:
M. Fuhrmann
Author:
K. Burgdorf
Author:
J. E. Baldwin
Author:
P. L. Roach
Author:
N. M. Shaw
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