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

BRENDA support

Literature summary for 5.1.1.13 extracted from

  • Liu, L.; Iwata, K.; Kita, A.; Kawarabayasi, Y.; Yohda, M.; Miki, K.
    Crystal structure of aspartate racemase from Pyrococcus horikoshii OT3 and its implications for molecular mechanism of PLP-independent racemization (2002), J. Mol. Biol., 319, 479-489.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapour diffusion method at 293 K, space group P21 with a: 65.5 A, b: 58.7 A, c: 67 A and beta 109.6° Pyrococcus horikoshii OT3

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate Pyrococcus horikoshii OT3 cell wall synthesis D-aspartate
-
?

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii OT3
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate
-
Pyrococcus horikoshii OT3 D-aspartate
-
?
L-aspartate cell wall synthesis Pyrococcus horikoshii OT3 D-aspartate
-
?

Subunits

Subunits Comment Organism
dimer crystallization studies Pyrococcus horikoshii OT3

Cofactor

Cofactor Comment Organism Structure
additional information not pyridoxal 5'phosphate dependent Pyrococcus horikoshii OT3