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Journal
2015 | 2 | 1 |
Article title

Functional investigation of Bacillus subtilis YrkF’s
involvement in sulfur transfer reactions

Content
Title variants
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EN
Abstracts
EN
Sulfur incorporation into the molybdenum
cofactor (Moco) in the Gram-negative bacterium
Escherichia coli involves six enzymes. The initial
reaction includes the cysteine desulfurase IscS, the
sulfurtransferase TusA, and the rhodanese domaincontaining
protein YnjE. The Gram-positive bacterium
Bacillus subtilis contains no direct homologs for IscS,
but rather four distinct cysteine desulfurases (YrvO, NifS,
NifZ, SufS) and YrkF, a two-domain rhodanese protein
with an N-terminal domain similar to TusA. Bioinformatic
analysis was used to identify potential enzymes involved
in the B. subtilis Moco thiolation pathway and in vitro
reactions demonstrated that YrkF can accept sulfur from
and enhance the activity of YrvO.
Publisher
Journal
Year
Volume
2
Issue
1
Physical description
Dates
online
20 - 1 - 2016
accepted
5 - 12 - 2015
received
6 - 8 - 2015
References
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Document Type
Publication order reference
YADDA identifier
bwmeta1.element.-psjd-doi-10_1515_ped-2015-0008
Identifiers
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