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Safety evaluation of the food enzyme asparaginase from the non‐genetically modified Saccharomyces cerevisiae strain ARY‐1

EFSA Journal
The asparaginase (l‐asparagine amidohydrolase, EC 3.5.1.1) is produced by the non‐genetically modified Saccharomyces cerevisiae strain ARY‐1 by Renaissance BioScience Corporation.
EFSA Panel on Food Enzymes (FEZ), Holger Zorn, José Manuel Barat Baviera, Claudia Bolognesi, Francesco Catania, Gabriele Gadermaier, Ralf Greiner, Baltasar Mayo, Alicja Mortensen, Yrjö Henrik Roos, Marize L. M. Solano, Monika Sramkova, Henk Van Loveren, Laurence Vernis, Jaime Aguilera, Daniele Cavanna, Cristina Fernàndez‐Fraguas, Yi Liu   +17 more
doaj   +1 more source

Crystallization and preliminary X-ray analysis of AAMS amidohydrolase, the final enzyme in degradation pathway i of pyridoxine [PDF]

, 2009
Kobayashi, Jun, Yoshida, Hiromi, Huy, Chu Nhat, Yoshikane, Yu, Kamitori, Shigehiro, Yagi, Toshiharu   +5 more
core   +1 more source

Uracil and beta-alanine degradation in Saccharomyces Kluyveri - discovery of a novel catabolic pathway [PDF]

, 2006
Andersen, Gorm
core  

Pyropheophytin a accompanies pheophytin a in darkened light grown cells of Euglena [PDF]

, 1981
Rüdiger, W., Scheer, Hugo, Schiff, J. A., Schoch, S., Siegelmann, H. W.   +4 more
core  

Putrescine is involved in Arabidopsis freezing tolerance and cold acclimation by regulating abscisic acid levels in response to low temperature [PDF]

, 2008
Alcázar, R., Altabella, T., Cuevas, J., Ferrando, A., Koncz, C., López-Cobollo, R., Salinas, J., Tiburcio, A., Zarza, X.   +8 more
core  

Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases

Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases
identifier:oai:t2r2.star.titech.ac.jp ...
openaire  

On the role of ethylene, auxin and a GOLVEN-like peptide hormone in the regulation of peach ripening [PDF]

core   +1 more source

Δ2,10-Phytodienol as esterifying alcohol of bacteriochlorophyll b from Ectothiorhodospira halochloris [PDF]

, 1981
Blos, I., Scheer, Hugo, Schäfer, W., Steiner, R., Wieschhoff, H.   +4 more
core  

Studies on Bacterial β-Aspartyl amidohydrolases

Studies on Bacterial β-Aspartyl amidohydrolases
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Dihydropyrimidine amidohydrolase is a zinc metalloenzyme

Biochimica Et Biophysica Acta - Biomembranes, 1979
Bovine liver dihydropyrimidine amidohydrolase (EC 3.5.2.2) has been subjected to atomic absorption analysis. Three different preparations of homogeneous enzyme indicated that the enzyme contains 4.3 +/- 0.3 g atoms of Zn2+ per mol of enzyme or 1.1 g atoms of Zn2+ per subunit. No Co2+, Mn2+, Mg2+ or Cd2+ was detected.
K P, Brooks, B D, Kim, E G, Sander
exaly   +3 more sources