Spinach glycolate oxidase

Lindqvist, Y. Refined structure of spinach glycolate oxidase at 2 A resolution. /. Mol. Biol. 209 ... 

Lindqvist, Y., Br%ondEn, C-L, Mathews, E. S., and Lederer, E., 1991, Spinach glycolate oxidase and yeast flavocytochrome foj sre structurally homologous and evolutionarily related enzymes wioth distinctly different function and EMN binding, J. Biol. Chem. 266 3198n3207. 

Macheroux, P., Kieweg, V., Massey, V., S derland, E., Stenberg, K., and Lindqvist, Y., 1993, Role of tyrosine 129 in the active site of spinach glycolate oxidase. Fur. J. Biochem. 213 1047nl054. 

Adam, W., Lazarus, M., Boss, B. et al. (1997) Enzymic resolution of chiral 2-hydroxy carboxylic acids by enantioselective oxidation with molecular oxygen catalyzed by the glycolate oxidase from spinach (Spinacia oleracea). The Journal of Organic Chemistry, 62 (22), 7841-7843. 

Fig. 4. Sequence alignment of flavocytochromes 62 and glycollate oxidase. The amino acid sequences of the mature forms of flavocytochromes 62 from Saccharomyces cerevisiae (Scb2) and Hansenula anomala (Hab2) and of glycollate oxidase from spinach (SpGO) are shown along with a consensus (Con) wherein all three sequences are identical. The interdomain hinge region and the proteinase-sensitive loop of flavocytochromes are boxed.

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