Partial Purification and Characterization of 1-Aminocyclopropane-1-Carboxylic Acid N-Malonyltransferase from Etiolated Mung Bean
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Partial Purification and Characterization of 1-Aminocyclopropane-1-Carboxylic Acid N-Malonyltransferase from Etiolated Mung Bean

Partial Purification and Characterization of 1-Aminocyclopropane-1-Carboxylic Acid N-Malonyltransferase from Etiolated Mung Bean


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About the Book

This dissertation, "Partial Purification and Characterization of 1-aminocyclopropane-1-carboxylic Acid N-malonyltransferase From Etiolated Mung Bean" by Chun-hang, Ma, 馬進恆, was obtained from The University of Hong Kong (Pokfulam, Hong Kong) and is being sold pursuant to Creative Commons: Attribution 3.0 Hong Kong License. The content of this dissertation has not been altered in any way. We have altered the formatting in order to facilitate the ease of printing and reading of the dissertation. All rights not granted by the above license are retained by the author. Abstract: Abstract of thesis entitled PARTIAL PURIFICATION AND CHARACTERIZATION OF 1-AMINOCYCLOPROPANE-1-CARBOXYLIC ACID N-MALONYLTRANSFERASE FROM ETIOLATED MUNG BEAN submitted by Ma Chun Hang for the degree of Master of Philosophy at The University of Hong Kong in August 2005 Ethylene is a plant hormone crucial in plant-growth regulation. The biosynthesis of ethylene is highly controlled and 1-aminocyclopropane-1-carboxylic acid (ACC) was identified as the direct precursor of ethylene. Besides being oxidized to ethylene, ACC also conjugates with malonyl coenzyme-A forming 1-(malonylamino)cyclopropane-1-carboxylic acid. The enzyme ACC N-malonyltransferase is responsible for this conjugation. Since the conjugation lowered ACC level in plant, the enzyme may play a regulatory role in ethylene production. Yet, there are still many uncertainties about the enzyme. In this project, a 7-step purification protocol for ACC N-malonyltransferase based mainly on liquid chromatography was introduced and ACC N-malonyltransferase was purified from etiolated mung bean hypocotyls by 230 fold. Two molecular forms of the enzyme were isolated with molecular mass of 70 kilodaltons and 36 kilodaltons. Subsequent characterizations showed that they shared the same optimal pH and temperature at pH 10.5 and 40 ℃ respectively. However, they show different responses towards D-amino acids. D-Amino acids, especially D-phenylalanine, exhibit greater inhibition on the 70 kilodaltons form. Though both forms confer ACC N-malonyltransferase activity, they have different kinetic parameters. The K values for ACC and malonyl Co-A of the heavier form are 170 and 260 μM respectively, while the K values for the same substrates of the lighter form are only 64 and 57 μM implying that the lighter form has a higher affinity towards ACC than the heavier form. This is the first time that more than one molecular forms of ACC N-malonyltransferase were identified in one single study. DOI: 10.5353/th_b3618134 Subjects: Enzymes - Analysis Chromatographic analysis Mung bean


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Product Details
  • ISBN-13: 9781361417270
  • Publisher: Open Dissertation Press
  • Publisher Imprint: Open Dissertation Press
  • Height: 279 mm
  • No of Pages: 122
  • Weight: 299 gr
  • ISBN-10: 1361417277
  • Publisher Date: 27 Jan 2017
  • Binding: Paperback
  • Language: English
  • Spine Width: 7 mm
  • Width: 216 mm


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Partial Purification and Characterization of 1-Aminocyclopropane-1-Carboxylic Acid N-Malonyltransferase from Etiolated Mung Bean
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