scholarly journals Research Note: Substrate Specificity of Duckling Hepatic and Renal D-Amino Acid Oxidase

1988 ◽  
Vol 67 (5) ◽  
pp. 851-854 ◽  
Author(s):  
R.G. ELKIN ◽  
M.L. LYONS
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Research Note ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

Engineering the Substrate Specificity of Porcine Kidney d-Amino Acid Oxidase by Mutagenesis of the “Active-Site Lid”

2006 ◽  
Vol 139 (5) ◽  
pp. 873-879 ◽  
Author(s):  
Chiaki Setoyama ◽  
Yasuzo Nishina ◽  
Hisashi Mizutani ◽  
Ikuko Miyahara ◽  
Ken Hirotsu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Active Site ◽  
Acid Oxidase ◽  
Porcine Kidney ◽  
Amino Acid Oxidase

Alteration of substrate specificity of fructosyl-amino acid oxidase from Fusarium oxysporum

2007 ◽  
Vol 74 (4) ◽  
pp. 813-819 ◽  
Author(s):  
Maki Fujiwara ◽  
Jun-ichi Sumitani ◽  
Shinji Koga ◽  
Issei Yoshioka ◽  
Takuji Kouzuma ◽  
...  
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Fusarium Oxysporum ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Fructosyl Amino Acid Oxidase

scholarly journals Engineering the Substrate Specificity ofd-Amino-acid Oxidase

2002 ◽  
Vol 277 (30) ◽  
pp. 27510-27516 ◽  
Author(s):  
Silvia Sacchi ◽  
Simona Lorenzi ◽  
Gianluca Molla ◽  
Mirella S. Pilone ◽  
Carlo Rossetti ◽  
...  
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

scholarly journals Amino Acid Catabolism by an areA-Regulated Gene Encoding an l-Amino Acid Oxidase with Broad Substrate Specificity in Aspergillus nidulans

2005 ◽  
Vol 71 (7) ◽  
pp. 3551-3555 ◽  
Author(s):  
Meryl A. Davis ◽  
Marion C. Askin ◽  
Michael J. Hynes
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Substrate Specificity ◽  
Nitrogen Source ◽  
Aspergillus Nidulans ◽  
Nitrogen Sources ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Broad Substrate Specificity ◽  
Strong Growth

ABSTRACT The filamentous fungus Aspergillus nidulans can use a wide range of compounds as nitrogen sources. The synthesis of the various catabolic enzymes needed to breakdown these nitrogen sources is regulated by the areA gene, which encodes a GATA transcription factor required to activate gene expression under nitrogen-limiting conditions. The areA102 mutation results in pleiotropic effects on nitrogen source utilization, including better growth on certain amino acids as nitrogen sources. Mutations in the sarA gene were previously isolated as suppressors of the strong growth of an areA102 strain on l-histidine as a sole nitrogen source. We cloned the sarA gene by complementation of a sarA mutant and showed that it encodes an l-amino acid oxidase enzyme with broad substrate specificity. Elevated expression of this enzyme activity in an areA102 background accounts for the strong growth of these strains on amino acids that are substrates for this enzyme. Loss of function sarA mutations, which abolish the l-amino acid oxidase activity, reverse the areA102 phenotype. Growth tests with areA102 and sarA mutants show that this enzyme is the primary route of catabolism for some amino acids, while other amino acids are metabolized through alternative pathways that yield either ammonium or glutamate for growth.

Alteration of substrate specificity of fructosyl-amino acid oxidase from Ulocladium sp. JS-103

2006 ◽  
Vol 102 (3) ◽  
pp. 241-243 ◽  
Author(s):  
Maki Fujiwara ◽  
Jun-ichi Sumitani ◽  
Shinji Koga ◽  
Issei Yoshioka ◽  
Takuji Kouzuma ◽  
...  
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Fructosyl Amino Acid Oxidase
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