2.6.1.30: pyridoxamine-pyruvate transaminase
This is an abbreviated version!
For detailed information about pyridoxamine-pyruvate transaminase, go to the full flat file.
Word Map on EC 2.6.1.30
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2.6.1.30
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pyridoxal
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mesorhizobium
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loti
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5'-phosphate
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transamination
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5'-deoxypyridoxal
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l-alanine
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pyridoxine
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nabh4
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4-oxidase
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analysis
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synthesis
- 2.6.1.30
- pyridoxal
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mesorhizobium
- loti
- 5'-phosphate
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transamination
- 5'-deoxypyridoxal
- l-alanine
- pyridoxine
- nabh4
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4-oxidase
- analysis
- synthesis
Reaction
Synonyms
aminotransferase, pyridoxamine-pyruvate, PM-pyruvate transaminase, PPAT, pyridoxamine-pyruvate aminotransferase, pyridoxamine-pyruvic transaminase
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Reaction
Reaction on EC 2.6.1.30 - pyridoxamine-pyruvate transaminase
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pyridoxamine + pyruvate = pyridoxal + L-alanine
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
pyridoxamine + pyruvate = pyridoxal + L-alanine
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
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