THIOL‐GLYOXYLATE ADDUCTS AS SUBSTRATES FOR RAT KIDNEY L‐α‐HYDROXY ACID OXIDASE *
THIOL‐GLYOXYLATE ADDUCTS AS SUBSTRATES FOR RAT KIDNEY L‐α‐HYDROXY ACID OXIDASE *
复制标题
硫醇-乙醛酸加合物作为大鼠肾 L-α-羟基酸氧化酶的底物 *
DOI:
10.1111/j.1749-6632.1982.tb21441.x
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发表时间:
1982
影响因子:
5.2
通讯作者:
G. A. Hamilton
中科院分区:
文献类型:
--
作者:
E. Brush;G. A. Hamilton
Peroxisomes are small organelles that characteristically contain catalase and several oxidative enzymes, including the flavoprotein oxidases, L-a-hydroxy acid oxidase (L-HAO) and D-aminO acid oxidase (D-AAO).'-~ Although these organelles are present in virtually all animal cells,' their metabolic function has remained unknown. The specific function of the flavoprotein oxidases has remained even more obscure because, until recently, no reasonable suggestion concerning the physiological substrates for these enzymes has been made, and the known, good substrates are not present to any significant extent physiologically. Recently we reported' that adducts of glyoxylate and various amines are substrates for D-AAO, and we presented arguments that the most likely physiological substrate for this enzyme is the cysteamine-glyoxylate adduct, thiazolidine-2-carboxylate. Because an adduct of any nucleophile with glyoxylate would be an a-hydroxy acid (eq. 1). X = 0, S, NH RXH + 0 = CH-COORX-CH-COO(1) I OH