Two Distinct L-Lactate Dehydrogenases Play a Role in the Survival of Neisseria gonorrhoeae in Cervical Epithelial Cells
2019 ◽
Vol 221
(3)
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pp. 449-453
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Keyword(s):
Abstract L-lactate is an abundant metabolite in a number of niches in host organisms and represents an important carbon source for bacterial pathogens such as Neisseria gonorrhoeae. In this study, we describe an alternative, iron-sulfur cluster-containing L-lactate dehydrogenase (LutACB), that is distinct from the flavoprotein L-lactate dehydrogenase (LldD). Expression of lutACB was found to be positively regulated by iron, whereas lldD was more highly expressed under conditions of iron-limitation. The functional role of LutACB and LldD was reflected in in vitro studies of growth and in the survival of N gonorrhoeae in primary cervical epithelial cells.
The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions
2020 ◽
Vol 295
(33)
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pp. 11891-11901
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2014 ◽
Vol 210
(8)
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pp. 1311-1318
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Keyword(s):
2007 ◽
Vol 283
(3)
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pp. 1362-1371
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Keyword(s):
2004 ◽
Vol 287
(2)
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pp. L448-L453
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Keyword(s):
2017 ◽
Vol 1861
(1)
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pp. 3154-3163
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