TY - JOUR
T1 - Synthesis of 3‐arsonoalanine and its action on aspartate aminotransferase and aspartate ammonia‐lyase
T2 - Comparison with arsenical analogues of malate and fumarate
AU - ALI, Bassam R.S.
AU - DIXON, Henry B.F.
PY - 1993/7
Y1 - 1993/7
N2 - dl‐3‐Arsonoalanine has been synthesized by the Strecker synthesis from the unstable compound arsonoacetaldehyde. It inactivates pig heart cytosolic aspartate aminotransferase and inhibits aspartate ammonia‐lyase by competing with aspartate (Ki/Km 0.23). The fumarate analogue (E)‐3‐arsonoacrylic acid and the malate analogue (RS)‐3‐arsonolactate also inhibit fumarate hydratase, competing with fumarate (Ki/Km 1.8) and malate (Ki/Km 1.6) respectively. Attempted non‐enzymic transamination of 3‐arsonoalanine gave elimination of arsenite, in contrast with the transamination of 3‐phosphonoalanine, which is either successful or leads to loss of phosphate.
AB - dl‐3‐Arsonoalanine has been synthesized by the Strecker synthesis from the unstable compound arsonoacetaldehyde. It inactivates pig heart cytosolic aspartate aminotransferase and inhibits aspartate ammonia‐lyase by competing with aspartate (Ki/Km 0.23). The fumarate analogue (E)‐3‐arsonoacrylic acid and the malate analogue (RS)‐3‐arsonolactate also inhibit fumarate hydratase, competing with fumarate (Ki/Km 1.8) and malate (Ki/Km 1.6) respectively. Attempted non‐enzymic transamination of 3‐arsonoalanine gave elimination of arsenite, in contrast with the transamination of 3‐phosphonoalanine, which is either successful or leads to loss of phosphate.
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U2 - 10.1111/j.1432-1033.1993.tb18018.x
DO - 10.1111/j.1432-1033.1993.tb18018.x
M3 - Article
C2 - 8344275
AN - SCOPUS:0027295528
SN - 0014-2956
VL - 215
SP - 161
EP - 166
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 1
ER -