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The fate of the carboxyl oxygens during D-proline reduction by clostridial proline reductase
- Source :
- Archives of biochemistry and biophysics. 311(2)
- Publication Year :
- 1994
-
Abstract
- D-Proline is converted to 5-amino valeric acid by D-proline reductase. This conversion involves the reductive cleavage of the α-carbon-nitrogen bond. We have examined the fate of the carboxyl oxygen atoms during conversion of D-proline to δ-NH2-valeric acid. 18O atoms from the carboxyl group of D-proline are not lost during conversion to product. In contrast, in the conversion of glycine to acetyl phosphate by glycine reductase a carboxyl oxygen atom is lost to solvent. An intermediate acyl-enzyme is found during the reduction of glycine. We conclude that the reduction of proline proceeds without the formation of an acyl enzyme intermediate.
- Subjects :
- Proline reductase
Valeric acid
Proline
Stereochemistry
Biophysics
Reductase
Oxygen Isotopes
Biochemistry
Glycine reductase
Mass Spectrometry
Substrate Specificity
chemistry.chemical_compound
Multienzyme Complexes
Organic chemistry
Molecular Biology
chemistry.chemical_classification
Clostridium
Stereoisomerism
Solvent
Enzyme
chemistry
Isotope Labeling
Glycine
Solvents
Amino Acid Oxidoreductases
Subjects
Details
- ISSN :
- 00039861
- Volume :
- 311
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Archives of biochemistry and biophysics
- Accession number :
- edsair.doi.dedup.....f324272b648ce5ca773439df625f90d9