On the presence of sepiapterin reductase different from folate and dihydrofolate reductase in chicken liver

1964 ◽  
Vol 20 (10) ◽  
pp. 574-575 ◽  
Author(s):  
M. Matsubara ◽  
M. Akino
Keyword(s):  
Dihydrofolate Reductase ◽  
Chicken Liver ◽  
Sepiapterin Reductase

Primary structure of chicken liver dihydrofolate reductase

Biochemistry ◽  
1980 ◽  
Vol 19 (4) ◽  
pp. 667-678 ◽  
Author(s):  
A. Ashok Kumar ◽  
Dale T. Blankenship ◽  
Bernard T. Kaufman ◽  
James H. Freisheim
Keyword(s):  
Dihydrofolate Reductase ◽  
Primary Structure ◽  
Chicken Liver

scholarly journals Activation of chicken liver dihydrofolate reductase by urea and guanidine hydrochloride is accompanied by conformational change at the active site

1996 ◽  
Vol 315 (1) ◽  
pp. 97-102 ◽  
Author(s):  
Ying-xin FAN ◽  
Ming JU ◽  
Jun-mei ZHOU ◽  
Chen-lu TSOU
Keyword(s):  
Catalytic Activity ◽  
Dihydrofolate Reductase ◽  
Conformational Changes ◽  
Active Site ◽  
Guanidine Hydrochloride ◽  
Chicken Liver ◽  
Peptide Fragments ◽  
Enhanced Fluorescence ◽  
Compact Structure ◽  
Mouse Leukaemia

It has been reported that the activation of dihydrofolate reductase (DHFR) from L1210 mouse leukaemia cells by KCl or thiol modifiers is accompanied by increased digestibility by proteinases [Duffy, Beckman, Peterson, Vitols and Huennekens (1987) J. Biol. Chem. 262, 7028–7033], suggesting a loosening up of the general compact structure of the enzyme. In the present study, the peptide fragments liberated from the chicken liver enzyme by digestion with trypsin in dilute solutions of urea or guanidine hydrochloride (GuHCl) have been separated by FPLC and sequenced. The sequences obtained are unique when compared with the known sequence of DHFR and thus allow the points of proteolytic cleavage identified for the urea- and GuHCl-activated enzyme to be at or near the active site. It was also indicated by the enhanced fluorescence of 2-p-toluidinylnaphthalene 6-sulphonate that conformational changes at the active site in dilute GuHCl parallel GuHCl activation. The above results indicate that the activation of DHFR in dilute denaturants is accompanied by a loosening up of its compact structure especially at or near the active site, suggesting that the flexibility at its active site is essential for the full expression of its catalytic activity.

scholarly journals Refined crystal structures of Escherichia coli and chicken liver dihydrofolate reductase containing bound trimethoprim.

1985 ◽  
Vol 260 (1) ◽  
pp. 381-391 ◽  
Author(s):  
D A Matthews ◽  
J T Bolin ◽  
J M Burridge ◽  
D J Filman ◽  
K W Volz ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Crystal Structures ◽  
Dihydrofolate Reductase ◽  
Chicken Liver
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