Flavin Binding to the High Affinity Riboflavin Transporter RibU
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چکیده
منابع مشابه
The riboflavin transporter RibU in Lactococcus lactis: molecular characterization of gene expression and the transport mechanism.
This study describes the characterization of the riboflavin transport protein RibU in the lactic acid bacterium Lactococcus lactis subsp. cremoris NZ9000. RibU is predicted to contain five membrane-spanning segments and is a member of a novel transport protein family, not described in the Transport Classification Database. Transcriptional analysis revealed that ribU transcription is downregulat...
متن کاملThe binding of flavin derivatives to the riboflavin-binding protein of egg white. A kinetic and thermodynamic study.
A method is described for the preparation and isolation of a riboflavin-binding protein in gram quantity. The product is found to be homogeneous in size and in binding character but slightly heterogeneous in net charge; it consists of a single polypeptide chain of about 30,000 daltons when examined by SDS gel electrophoresis. An affinity chromatography method is described by which flavin analog...
متن کاملCharacterization of riboflavin (vitamin B2) transport proteins from Bacillus subtilis and Corynebacterium glutamicum.
Riboflavin (vitamin B(2)) is the direct precursor of the flavin cofactors flavin mononucleotide and flavin adenine dinucleotide, essential components of cellular biochemistry. In this work we investigated the unrelated proteins YpaA from Bacillus subtilis and PnuX from Corynebacterium glutamicum for a role in riboflavin uptake. Based on the regulation of the corresponding genes by a riboswitch ...
متن کاملLow Affinity and Slow Na+ Binding Precedes High Affinity Aspartate Binding in the Secondary-active Transporter GltPh.
GltPh from Pyrococcus horikoshii is a homotrimeric Na(+)-coupled aspartate transporter. It belongs to the widespread family of glutamate transporters, which also includes the mammalian excitatory amino acid transporters that take up the neurotransmitter glutamate. Each protomer in GltPh consists of a trimerization domain involved in subunit interactions and a transport domain containing the sub...
متن کاملUse of riboflavin-binding protein to investigate steric and electronic relationships in flavin analogs and models.
We have examined the affinity of two recently synthesized flavin analogs for the isoalloxazine binding site of riboflavin-binding protein (RBP). The results showed that pyrimidopteridines could bind to RBP (Kd 160-250 microM). This suggested that, at the FMN or FAD level, these analogs might also bind to other apoflavoproteins, thereby providing a high potential probe for flavin enzymology. In ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2007
ISSN: 0021-9258
DOI: 10.1074/jbc.m608583200