Properties of Rhodotorula gracilis d-Amino Acid Oxidase Immobilized on Magnetic Beads through His-Tag

2008 ◽  
Vol 105 (2) ◽  
pp. 110-115 ◽  
Author(s):  
Iching Kuan ◽  
Renjie Liao ◽  
Haochieh Hsieh ◽  
Kuanchun Chen ◽  
Chiyang Yu
Keyword(s):  
Amino Acid ◽  
Magnetic Beads ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
His Tag ◽  
Rhodotorula Gracilis

Effect of hydrogen peroxide on d-amino acid oxidase from Rhodotorula gracilis

2000 ◽  
Vol 27 (3-5) ◽  
pp. 234-239 ◽  
Author(s):  
Isabel de la Mata ◽  
Fernando Ramón ◽  
Virginia Obregón ◽  
Ma Pilar Castillón ◽  
Carmen Acebal
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Rhodotorula Gracilis

scholarly journals Chemical mechanism of D-amino acid oxidase from Rhodotorula gracilis: pH dependence of kinetic parameters

1998 ◽  
Vol 330 (1) ◽  
pp. 311-314 ◽  
Author(s):  
F. RAMÓN ◽  
M. P. CASTILLÓN ◽  
I. DE LA MATA ◽  
C. ACEBAL
Keyword(s):  
Amino Acid ◽  
Kinetic Parameters ◽  
Ph Dependence ◽  
Competitive Inhibitor ◽  
Chemical Mechanism ◽  
Acid Oxidase ◽  
Protonation State ◽  
Amino Acid Oxidase ◽  
Basic Group ◽  
Rhodotorula Gracilis

The variation of kinetic parameters of D-amino acid oxidase from Rhodotorula gracilis with pH was used to gain information about the chemical mechanism of the oxidation of D-amino acids catalysed by this flavoenzyme. D-Alanine was the substrate used. The pH dependence of Vmax and Vmax/Km for alanine as substrate showed that a group with a pK value of 6.26-7.95 (pK1) must be unprotonated and a group with a pK of 10.8-9.90 (pK2) must be protonated for activity. The lower pK value corresponded to a group on the enzyme involved in catalysis and whose protonation state was not important for binding. The higher pK value was assumed to be the amino group of the substrate. Profiles of pKi for D-aspartate as competitive inhibitor showed that binding is prevented when a group on the enzyme with a pK value of 8.4 becomes unprotonated; this basic group was not detected in Vmax/Km profiles suggesting its involvement in binding of the β-carboxylic group of the inhibitor.

scholarly journals High-level expression of Rhodotorula gracilis d-amino acid oxidase in Pichia pastoris

2010 ◽  
Vol 33 (3) ◽  
pp. 557-563 ◽  
Author(s):  
Sandra Abad ◽  
Jozef Nahalka ◽  
Margit Winkler ◽  
Gabriele Bergler ◽  
Robert Speight ◽  
...  
Keyword(s):  
Amino Acid ◽  
Pichia Pastoris ◽  
Acid Oxidase ◽  
High Level Expression ◽  
Amino Acid Oxidase ◽  
Rhodotorula Gracilis ◽  
High Level

ON THE RECOMBINATION PROCESS OF APO-D-AMINO ACID OXIDASE FROM Rhodotorula gracilis

1991 ◽  
pp. 171-174
Author(s):  
Paola Casalin ◽  
Loredano Pollegioni ◽  
Bruno Curti ◽  
Mirella Pilone Simonetta
Keyword(s):  
Amino Acid ◽  
Recombination Process ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Rhodotorula Gracilis

scholarly journals Properties of D-amino-acid oxidase from Rhodotorula gracilis

1989 ◽  
Vol 180 (1) ◽  
pp. 199-204 ◽  
Author(s):  
Mirella PILONE SIMONETTA ◽  
Loredano POLLEGIONI ◽  
Paola CASALIN ◽  
Bruno CURTI ◽  
Severino RONCHI
Keyword(s):  
Amino Acid ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Rhodotorula Gracilis

scholarly journals A study on apoenzyme from Rhodotorula gracilis D-amino acid oxidase

1991 ◽  
Vol 197 (2) ◽  
pp. 513-517 ◽  
Author(s):  
Paola CASALIN ◽  
Loredano POLLEGIONI ◽  
Bruno CURTI ◽  
Mirella PILONE SIMONETTA
Keyword(s):  
Amino Acid ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Rhodotorula Gracilis

scholarly journals Tryptophan 243 affects interprotein contacts, cofactor binding and stability in D-amino acid oxidase from Rhodotorula gracilis

FEBS Journal ◽  
2006 ◽  
Vol 273 (3) ◽  
pp. 504-512 ◽  
Author(s):  
Laura Caldinelli ◽  
Gianluca Molla ◽  
Mirella S. Pilone ◽  
Loredano Pollegioni
Keyword(s):  
Amino Acid ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Cofactor Binding ◽  
Rhodotorula Gracilis
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