Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Reaction

pyridoxamine
+
pyruvate
=
pyridoxal
+
L-alanine

Synonyms

aminotransferase, pyridoxamine-pyruvate, PM-pyruvate transaminase, PPAT, pyridoxamine-pyruvate aminotransferase, pyridoxamine-pyruvic transaminase

ECTree

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.30 pyridoxamine-pyruvate transaminase

Crystallization

Crystallization on EC 2.6.1.30 - pyridoxamine-pyruvate transaminase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
addition of saturated ammonium sulfate solution to the concentrated protein solution until the first permanent turbidity appears, several days at 5°C
-