Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
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Enzyme
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Query: UNIPROT:P50583 (
asymmetrical
)
12,197
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Propionate kinase catalyses the last step in the anaerobic breakdown of L-threonine to propionate in which propionyl phosphate and ADP are converted to propionate and ATP. Here we report the structures of
propionate kinase
(
TdcD
) in the native form as well as in complex with
diadenosine 5',5'''-P1,P4-tetraphosphate
(Ap4A) by X-ray crystallography. Structure of
TdcD
obtained after cocrystallization with ATP showed Ap4A bound to the active site pocket suggesting the presence of Ap4A synthetic activity in
TdcD
. Binding of Ap4A to the enzyme was confirmed by the structure determination of a
TdcD
-Ap4A complex obtained after cocrystallization of
TdcD
with commercially available Ap4A. Mass spectroscopic studies provided further evidence for the formation of Ap4A by
propionate kinase
in the presence of ATP. In the
TdcD
-Ap4A complex structure, Ap4A is present in an extended conformation with one adenosine moiety present in the nucleotide binding site and other in the proposed propionate binding site. These observations tend to support direct in-line transfer of phosphoryl group during the kinase reaction.
...
PMID:Crystal structures of Salmonella typhimurium propionate kinase and its complex with Ap4A: evidence for a novel Ap4A synthetic activity. 1789 50
