Si-face stereospecificity at C5 of coenzyme F420 for F420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis and F420-dependent alcohol dehydrogenase from Methanoculleus thermophilicus.
Eur J Biochem
; 239(1): 93-7, 1996 Jul 01.
Article
in En
| MEDLINE
| ID: mdl-8706724
ABSTRACT
Coenzyme F420 is a 5-deazaflavin. Upon reduction, 1,5-dihydro-coenzyme F420 is formed with a prochiral center at C5. In this study we report that the F420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis and the F420-dependent alcohol dehydrogenase from Methanoculleus thermophilicus are Si-face stereospecific with respect to C5 of the 5-deazaflavin. These results were obtained by following the stereochemical course of the reversible incorporation of 3H into F420 from tritium-labeled substrates. Our findings bring to eight the number of coenzyme-F420-dependent enzymes shown to be Si-face stereospecific. No F420-dependent enzyme with Re-face stereospecificity is known. This is noteworthy since coenzyme F420 is functionally similar to pyridine nucleotides for which both Si-face and Re-face specific enzymes have been found.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Riboflavin
/
Alcohol Dehydrogenase
/
Euryarchaeota
/
Glucosephosphate Dehydrogenase
/
Mycobacterium
Language:
En
Journal:
Eur J Biochem
Year:
1996
Type:
Article
Affiliation country:
Germany