Abstract:
:Cystalysin, the key virulence factor in the bacterium Treponema denticola responsible for periodontis, is a pyridoxal 5'-phosphate (PLP) enzyme which catalyzes, in addition to alpha,beta-elimination of L-cysteine, racemization and transamination of both enantiomers of alanine. In this paper several indicators have been used as probes of the different conformational status of T. denticola cystalysin in the holo and apo form. Compared to holoenzyme, the apoenzyme displays an altered reactivity of cysteine residues, a significantly different pI, and a differential susceptibility to proteinase K. The site of cleavage that is accessible in apocystalysin and masked in holocystalysin has been identified by mass spectrometry as the peptide bond between Phe 360 and Gly 361. This cleavage results in the loss of the C-terminal fragment corresponding to a molecular mass of 4289.21+/-0.1Da. The major fragment of cleaved enzyme retains its dimeric structure, binds the coenzyme with an affinity approximately 5000-fold lower than that of uncleaved holoenzyme, and in the reconstituted form is able to form the external aldimine with substrates. Although the break causes the loss of lyase, racemase and transaminase activities of D-alanine, it does not abolish the transaminase activity of L-alanine. Possible mechanistic and physiological implications are proposed.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Cellini B,Montioli R,Bossi A,Bertoldi M,Laurents DV,Voltattorni CBdoi
10.1016/j.abb.2006.08.020subject
Has Abstractpub_date
2006-11-01 00:00:00pages
31-9issue
1eissn
0003-9861issn
1096-0384pii
S0003-9861(06)00310-9journal_volume
455pub_type
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journal_title:Archives of biochemistry and biophysics
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