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Selenalysine transamination by a bovine brain enzyme
C Blarzino1, R Coccia, C Foppoli
1Dipartimento di Scienze Biochimiche, Università La Sapienza, Roma, Italy.
Physiological Chemistry and Physics and Medical NMR
|January 1, 1989
Summary
Bovine brain glutamine transaminase deaminates selenyl-lysine, forming an alpha-ketoacid that cyclizes into a ketimine. Selenyl-lysine exhibits strong binding affinity to this enzyme.
Area of Science:
- Biochemistry
- Enzymology
- Amino Acid Metabolism
Background:
- Glutamine transaminase is a key enzyme in amino acid metabolism.
- Selenalysine is a selenium-containing analog of lysine.
Purpose of the Study:
- To investigate the enzymatic deamination of selenyl-lysine by glutamine transaminase from bovine brain.
- To characterize the reaction products and enzyme-substrate interactions.
Main Methods:
- Enzymatic assays using purified glutamine transaminase from bovine brain.
- Incubation of selenyl-lysine with the enzyme.
- Analysis of reaction products using spectroscopic methods.
Main Results:
- Selenalysine undergoes deamination catalyzed by bovine brain glutamine transaminase.
- The reaction yields the corresponding alpha-ketoacid of selenyl-lysine.
- The alpha-ketoacid spontaneously cyclizes to a ketimine form.
- Selenalysine demonstrated a significant affinity for the glutamine transaminase enzyme.
Conclusions:
- Glutamine transaminase effectively processes selenyl-lysine.
- The enzymatic activity leads to the formation of a unique ketimine structure.
- The findings highlight the enzyme's substrate specificity and potential role in seleno-amino acid metabolism.