enzyme first binds pyridoxamine and then forms a Michaelis complex with the incoming pyruvate. The ketimine is formed through nucleophilic attack of the N-4' atom of pyridoxamine on the alpha-carbon atom of pyruvate, which is followed by the release of a water molecule. The stereospecific 1,3-prototropic shift between the ketimine and external aldimine via the quinonoid intermediate is accomplished through general base catalysis by Lys197. Pyridoxal and L-alanine are formed from the external aldimine and released from enzyme
enzyme first binds pyridoxamine and then forms a Michaelis complex with the incoming pyruvate. The ketimine is formed through nucleophilic attack of the N-4' atom of pyridoxamine on the alpha-carbon atom of pyruvate, which is followed by the release of a water molecule. The stereospecific 1,3-prototropic shift between the ketimine and external aldimine via the quinonoid intermediate is accomplished through general base catalysis by Lys197. Pyridoxal and L-alanine are formed from the external aldimine and released from enzyme
the enzyme shows less than 0.5% of the activity of pyridoxamine towards pyridoxamine 5'-phosphate (3.3 mM) with pyruvate as the amino acceptor, the enzyme shows less than 0.5% of the activity of pyruvate towards 2-oxoglutarate, 3-hydroxypyruvate, indol-pyruvate, phenylpyruvate, 3-methyl-2-oxobutyrate and 4-hydroxyphenylpyruvate when they are used at 10 mM
the enzyme shows less than 0.5% of the activity of pyridoxamine towards pyridoxamine 5'-phosphate (3.3 mM) with pyruvate as the amino acceptor, the enzyme shows less than 0.5% of the activity of pyruvate towards 2-oxoglutarate, 3-hydroxypyruvate, indol-pyruvate, phenylpyruvate, 3-methyl-2-oxobutyrate and 4-hydroxyphenylpyruvate when they are used at 10 mM
the enzyme shows less than 0.5% of the activity of pyridoxamine towards pyridoxamine 5'-phosphate (3.3 mM) with pyruvate as the amino acceptor, the enzyme shows less than 0.5% of the activity of pyruvate towards 2-oxoglutarate, 3-hydroxypyruvate, indol-pyruvate, phenylpyruvate, 3-methyl-2-oxobutyrate and 4-hydroxyphenylpyruvate when they are used at 10 mM
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme, space group P43212, diffraction to 2.0 A resolution. Complexes with pyridoxamine, pyridoxal, and pyridoxyl-L-alanine at 1.7 A, 1.7 A, and 2.0 A resolution, respectively. Enzyme is a homotetramer and each subunit is composed of a large N-terminal domain, consisting of seven beta-sheets and eight alpha-helices, and a smaller C-terminal domain, consisting of three beta-sheets and four alpha-helices. The substrate pyridoxal is bound through an aldimine linkage to Lys197 in the active site. The carboxylate group of the substrate amino/keto acid is hydrogen-bonded to Arg336 and Arg345
pyridoxamine is produced from pyridoxine by bioconversion using a Rhodococcus expression system. Approximately 450 mM pyridoxal are produced from 500 mM pyridoxine using recombinant Rhodococcus erythropolis expressing the pyridoxine 4-oxidase gene derived from Mesorhizobium loti. In the bioconversion of pyridoxal to pyridoxamine using recombinant Rhodococcus erythropolis expressing the pyridoxamine-pyruvate aminotransferase gene derived from Mesorhizobium loti, the bioconversion rate is approximately 80% under the same conditions as pyridoxal production. Finally, in the bioconversion of pyridoxine to pyridoxamine through pyridoxal using recombinant Rhodococcus erythropolis coexpressing the genes for pyridoxine 4-oxidase and pyridoxamine-pyruvate aminotransferase, the bioconversion rate is approximately 75%. Reactor bioconversion using the Rhodococcus expression system, method evaluation and optimization, overview
pyridoxamine is produced from pyridoxine by bioconversion using a Rhodococcus expression system. Approximately 450 mM pyridoxal are produced from 500 mM pyridoxine using recombinant Rhodococcus erythropolis expressing the pyridoxine 4-oxidase gene derived from Mesorhizobium loti. In the bioconversion of pyridoxal to pyridoxamine using recombinant Rhodococcus erythropolis expressing the pyridoxamine-pyruvate aminotransferase gene derived from Mesorhizobium loti, the bioconversion rate is approximately 80% under the same conditions as pyridoxal production. Finally, in the bioconversion of pyridoxine to pyridoxamine through pyridoxal using recombinant Rhodococcus erythropolis coexpressing the genes for pyridoxine 4-oxidase and pyridoxamine-pyruvate aminotransferase, the bioconversion rate is approximately 75%. Reactor bioconversion using the Rhodococcus expression system, method evaluation and optimization, overview
pyridoxamine is produced from pyridoxine by bioconversion using a Rhodococcus expression system. Approximately 450 mM pyridoxal are produced from 500 mM pyridoxine using recombinant Rhodococcus erythropolis expressing the pyridoxine 4-oxidase gene derived from Mesorhizobium loti. In the bioconversion of pyridoxal to pyridoxamine using recombinant Rhodococcus erythropolis expressing the pyridoxamine-pyruvate aminotransferase gene derived from Mesorhizobium loti, the bioconversion rate is approximately 80% under the same conditions as pyridoxal production. Finally, in the bioconversion of pyridoxine to pyridoxamine through pyridoxal using recombinant Rhodococcus erythropolis coexpressing the genes for pyridoxine 4-oxidase and pyridoxamine-pyruvate aminotransferase, the bioconversion rate is approximately 75%. Reactor bioconversion using the Rhodococcus expression system, method evaluation and optimization, overview
gene ppaT, functional recombinant expression of soluble enzyme in Rhodococcus erythropolis strain JCM3191, co-expression with pyridoxine 4-oxidase (PNO) from Mesorhizobium loti from gene pno
determination method for individual natural vitamin B6 compounds. Compounds are specifically converted into 4-pyridoxolactone by pyridoxal 4-dehydrogenase and coupling reactions involving pyridoxine 4-oxidase, pyridoxal 4-dehydrogenase, or pyridoxamine-pyruvate aminotransferase and pyridoxal 4-dehydrogenase. Application of method for analysis of food samples
pyridoxamine production by bioconversion is generally preferable for environmental and energetic aspects compared to chemical synthesis. Pyridoxamine is produced from pyridoxine, a readily and economically available starting material, by bioconversion using a Rhodococcus expression system
pyridoxamine production by bioconversion is generally preferable for environmental and energetic aspects compared to chemical synthesis. Pyridoxamine is produced from pyridoxine, a readily and economically available starting material, by bioconversion using a Rhodococcus expression system
pyridoxamine production by bioconversion is generally preferable for environmental and energetic aspects compared to chemical synthesis. Pyridoxamine is produced from pyridoxine, a readily and economically available starting material, by bioconversion using a Rhodococcus expression system
Pyridoxamine-pyruvate transaminase. 1. Determination of the active site stoichiometry and the pH dependence of the dissociation constant for 5-deoxypyridoxal
Pyridoxamine-pyruvate transaminase. 2. Temperature-jump and stopped-flow kinetic investigation of the rates and mechanism of the reaction of 5-deoxypyridoxal with the enzyme
Vitamin B6 degradation by pyridoxamine-pyruvate transaminase and pyridoxine 4-oxidase from Ochrobactrum anthropi- and Enterobacter cloacae-like bacteria