Abstract:
:Rhodospirillum rubrum ribulose bisphosphate carboxylase contains two high affinity binding sites for pyridoxal phosphate and two catalytic sites per dimer. However, pyridoxal phosphate binding at only one site is sufficient for inactivation of both catalytic sites. In the presence of 20 mM bicarbonate, 10 mM magnesium, and pyridoxal phosphate, the rates of inactivation and Schiff base formation are pseudo-first-order and show saturation kinetics. These observations provide additional evidence that pyridoxal phosphate binds at the active site of the R. rubrum carboxylase. It is also proposed that the large subunit may contain regulatory as well as catalytic properties.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Whitman WB,Tabita FRdoi
10.1021/bi00600a024subject
Has Abstractpub_date
1978-04-04 00:00:00pages
1288-93issue
7eissn
0006-2960issn
1520-4995journal_volume
17pub_type
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