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来自假单胞菌AM1的苹果酰辅酶A裂解酶的纯化及性质

Purification and properties of malyl-coenzyme A lyase from Pseudomonas AM1.

作者信息

Hacking A J, Quayle J R

出版信息

Biochem J. 1974 May;139(2):399-405. doi: 10.1042/bj1390399.

DOI:10.1042/bj1390399
PMID:4447618
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1166296/
Abstract
  1. Malyl-CoA lyase was purified 20-fold from extracts of methanol-grown Pseudomonas AM1. 2. Preparations of the enzyme were essentially homogeneous by electrophoretic and ultracentrifugal criteria. 3. Malyl-CoA lyase has a molecular weight of 190000 determined from sedimentation-equilibrium data. 4. Within the range of compounds tested, malyl-CoA lyase is specific for (2S)-4-malyl-CoA or glyoxylate and acetyl-CoA or propionyl-CoA. 5. A bivalent cation is essential for activity, Mg(2+) or Co(2+) being most effective. 6. Malyl-CoA lyase is inhibited by (2R)-4-malyl-CoA and by some buffers, but thiol-group inhibitors are without effect. 7. Optimal activity was recorded at pH7.8. 8. An equilibrium constant of 4.7x10(-4)m was determined for the malyl-CoA cleavage reaction. 9. The Michaelis constants for the enzyme are: 4-malyl-CoA, 6.6x10(-5)m; acetyl-CoA, 1.5x10(-5)m; glyoxylate, 1.7x10(-3)m; Mg(2+), 1.2x10(-3)m.
摘要

  1. 从甲醇培养的假单胞菌AM1提取物中纯化出20倍的苹果酰辅酶A裂合酶。

  2. 根据电泳和超速离心标准，该酶制剂基本均一。

  3. 根据沉降平衡数据测定，苹果酰辅酶A裂合酶的分子量为190000。

  4. 在测试的化合物范围内，苹果酰辅酶A裂合酶对(2S)-4-苹果酰辅酶A或乙醛酸以及乙酰辅酶A或丙酰辅酶A具有特异性。

  5. 二价阳离子对活性至关重要，Mg(2+)或Co(2+)最为有效。

  6. 苹果酰辅酶A裂合酶受到(2R)-4-苹果酰辅酶A和某些缓冲液的抑制，但巯基抑制剂无效。

  7. 在pH7.8时记录到最佳活性。

  8. 测定苹果酰辅酶A裂解反应的平衡常数为4.7×10(-4)m。

  9. 该酶的米氏常数为：4-苹果酰辅酶A，6.6×10(-5)m；乙酰辅酶A，1.5×10(-5)m；乙醛酸，1.7×10(-3)m；Mg(2+)，1.2×10(-3)m。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d4ac/1166296/7b126d3ab774/biochemj00584-0128-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d4ac/1166296/7b126d3ab774/biochemj00584-0128-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d4ac/1166296/7b126d3ab774/biochemj00584-0128-a.jpg

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