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
ECTree
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Crystallization
Crystallization on EC 2.6.1.30 - pyridoxamine-pyruvate transaminase
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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
addition of saturated ammonium sulfate solution to the concentrated protein solution until the first permanent turbidity appears, several days at 5°C
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