PMID- 1100371
OWN - NLM
STAT- MEDLINE
DCOM- 19751211
LR  - 20190620
IS  - 0014-2956 (Print)
IS  - 0014-2956 (Linking)
VI  - 52
IP  - 1
DP  - 1975 Mar 3
TI  - Fluorescence studies on the interaction between yeast seryl-tRNA synthetase and 
      its substrates.
PG  - 171-8
AB  - Substrate-induced variations in the native fluorescence of seryl-tRNA synthetase 
      from yeast have been used to evaluate the binding equilibria with its ligands. 
      Binding of L-serine to the enzyme can be detected by equilibrium dialysis but not 
      by fluorescence quenching. Hence, in contrast to ATP and tRNA(Ser), L-serine does 
      not induce any fluorescence-sensitive conformational change of the synthetase. A 
      comparison of the binding constants for ATP (2 X10(4) M-1) and seryl adenylate (1 
      x10(6) M-1) indicates that the activation reaction is mainly driven by the higher 
      affinity of seryl adenylate to the enzyme. tRNA(Ser) and seryl-tRNA(Ser) though 
      causing rather different maximal fluorescence quenching are bound to the enzyme 
      with similar stoichiometry and association constant. The implications of this 
      result are discussed with respect to the mechanism of the aminoacylation 
      reaction. It is also shown that the enzyme clearly is capable of discriminating 
      L-serine from other amino acids, ATP from other nucleotidetriphosphates and AMP, 
      and tRNA(SER) from other tRNA species in the binding processes. The spectral 
      properties, the effects of outside quenchers and the fluorescence decay times of 
      the free enzyme and the enzyme-substrate complexes are discussed with respect to 
      the intercalation hypothesis of Helene.
FAU - Maelicke, A
AU  - Maelicke A
FAU - Cramer, F
AU  - Cramer F
LA  - eng
PT  - Journal Article
PL  - England
TA  - Eur J Biochem
JT  - European journal of biochemistry
JID - 0107600
RN  - 452VLY9402 (Serine)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - 9014-25-9 (RNA, Transfer)
RN  - EC 6.1.1.- (Amino Acyl-tRNA Synthetases)
RN  - EC 6.1.1.11 (Serine-tRNA Ligase)
SB  - IM
MH  - Adenosine Triphosphate/pharmacology
MH  - Amino Acyl-tRNA Synthetases/*metabolism
MH  - Binding Sites
MH  - Dialysis
MH  - Kinetics
MH  - Protein Binding
MH  - RNA, Transfer
MH  - Saccharomyces cerevisiae/*enzymology
MH  - Serine
MH  - Serine-tRNA Ligase/*metabolism
MH  - Spectrometry, Fluorescence
EDAT- 1975/03/03 00:00
MHDA- 1975/03/03 00:01
CRDT- 1975/03/03 00:00
PHST- 1975/03/03 00:00 [pubmed]
PHST- 1975/03/03 00:01 [medline]
PHST- 1975/03/03 00:00 [entrez]
AID - 10.1111/j.1432-1033.1975.tb03984.x [doi]
PST - ppublish
SO  - Eur J Biochem. 1975 Mar 3;52(1):171-8. doi: 10.1111/j.1432-1033.1975.tb03984.x.