scholarly journals The ubiquitous cofactor NADH protects against substrate-induced inhibition of a pyridoxal enzyme

1996 ◽  
Vol 5 (12) ◽  
pp. 2545-2551 ◽  
Author(s):  
Wanda M. Jones ◽  
Peter W. Van Ophem ◽  
Maria A. Pospischil ◽  
Dagmar Ringe ◽  
Gregory Petsko ◽  
...  
Keyword(s):  
Pyridoxal Enzyme

Inhibitory activity of 4-vinyl analogs of pyridoxal: enzyme and cell culture studies

Biochemistry ◽  
1976 ◽  
Vol 15 (25) ◽  
pp. 5458-5466 ◽  
Author(s):  
W. Korytnyk ◽  
M. T. Hakala ◽  
P. G. G. Potti ◽  
N. Angelino ◽  
S. C. Chang
Keyword(s):  
Cell Culture ◽  
Inhibitory Activity ◽  
Culture Studies ◽  
Pyridoxal Enzyme

scholarly journals X-Ray snapshots of a pyridoxal enzyme: a catalytic mechanism involving concerted [1,5]-hydrogen sigmatropy in methionine γ-lyase

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Dan Sato ◽  
Tomoo Shiba ◽  
Tsuyoshi Karaki ◽  
Wataru Yamagata ◽  
Tomoyoshi Nozaki ◽  
...  
Keyword(s):  
Catalytic Mechanism ◽  
X Ray ◽  
Pyridoxal Enzyme

A novel zinc-dependent D-serine dehydratase from Saccharomyces cerevisiae

2007 ◽  
Vol 409 (2) ◽  
pp. 399-406 ◽  
Author(s):  
Tomokazu Ito ◽  
Hisashi Hemmi ◽  
Kunishige Kataoka ◽  
Yukio Mukai ◽  
Tohru Yoshimura
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Alanine Racemase ◽  
Absorption Analysis ◽  
Edta Treatment ◽  
Putative Protein ◽  
Escherichia Coli Cells ◽  
Bacterial Enzyme ◽  
Serine Dehydratase ◽  
Pyridoxal Enzyme

YGL196W of Saccharomyces cerevisiae encodes a putative protein that is unidentified but is predicted to have a motif similar to that of the N-terminal domain of the bacterial alanine racemase. In the present study we found that YGL196W encodes a novel D-serine dehydratase, which belongs to a different protein family from that of the known bacterial enzyme. The yeast D-serine dehydratase purified from recombinant Escherichia coli cells depends on pyridoxal 5′-phosphate and zinc, and catalyses the conversion of D-serine into pyruvate and ammonia with the Km and kcat values of 0.39 mM and 13.1 s−1 respectively. D-Threonine and β-Cl-D-alanine also serve as substrates with catalytic efficiencies which are approx. 3 and 2% of D-serine respectively. L-Serine, L-threonine and β-Cl-L-alanine are inert as substrates. Atomic absorption analysis revealed that the enzyme contains one zinc atom per enzyme monomer. The enzyme activities toward D-serine and D-threonine were decreased by EDTA treatment and recovered by the addition of Zn2+. Little recovery was observed with Mg2+, Mn2+, Ca2+, Ni2+, Cu2+, K+ or Na+. In contrast, the activity towards β-Cl-D-alanine was retained after EDTA treatment. These results suggest that zinc is involved in the elimination of the hydroxy group of D-serine and D-threonine. D-Serine dehydratase of S. cerevisiae is probably the first example of a eukaryotic D-serine dehydratase and that of a specifically zinc-dependent pyridoxal enzyme as well.

scholarly journals A Novel Metal-activated Pyridoxal Enzyme with a Unique Primary Structure, Low Specificity d-Threonine Aldolase fromArthrobactersp. Strain DK-38

1998 ◽  
Vol 273 (27) ◽  
pp. 16678-16685 ◽  
Author(s):  
Ji-Quan Liu ◽  
Tohru Dairi ◽  
Nobuya Itoh ◽  
Michihiko Kataoka ◽  
Sakayu Shimizu ◽  
...  
Keyword(s):  
Primary Structure ◽  
Threonine Aldolase ◽  
Pyridoxal Enzyme
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