Reversible inhibition by pyridoxal 5'-phosphate and irreversible inactivation by urea and guanidine hydrochloride of thymidylate synthase from Lactobacillus leichmannii.
Indian J Biochem Biophys
; 1998 Aug; 35(4): 229-35
Article
in En
| IMSEAR
| ID: sea-28159
ABSTRACT
Pyridoxal 5'-phosphate reversibly inhibited thymidylate synthase from Lactobacillus leichmannii. The inhibition was competitive with dUMP (Ki = 1 microM) and non-competitive with 5,10-CH2-THF (Ki = 0.08 microM). Treatment of native or pCMB-treated enzyme with urea (5 M) or guanidine hydrochloride (4 M) resulted in inactivation and dissociation of the homodimer (74 kDa) into monomer (37 kDa).
Full text:
1
Index:
IMSEAR
Main subject:
Protein Conformation
/
Pyridoxal Phosphate
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Thymidylate Synthase
/
Urea
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Dimerization
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Guanidine
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Enzyme Inhibitors
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Lactobacillus
Language:
En
Journal:
Indian J Biochem Biophys
Year:
1998
Type:
Article