Auxin‐conjugate hydrolysis in Chinese cabbage: characterization of an amidohydrolase and its role during infection with clubroot disease (Record no. 55488)

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control field MX-MdCICY
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control field 20250626080924.0
040 ## - CATALOGING SOURCE
Transcribing agency CICY
090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN)
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-32
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245 10 - TITLE STATEMENT
Title Auxin‐conjugate hydrolysis in Chinese cabbage: characterization of an amidohydrolase and its role during infection with clubroot disease
490 0# - SERIES STATEMENT
Series statement Physiol Plant, 97(4), p.627-634, 1996
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General note Artículo
520 3# - SUMMARY, ETC.
Summary, etc. Auxin conjugates play a role in the regulation of free indole-3-acetic acid (IAA) content in plants. Not much is known about the enzymes involved in either conjugate synthesis or hydrolysis. In this study we have isolated and characterized an auxin conjugate hydrolase from Chinese cabbage seedlings and investigated it during the development of both the Chinese cabbage plants and the clubroot disease. The hydrolase isolated from light- and dark-grown seedlings accepted the amide conjugates indole-3-acetic acid-alanine (IAAla), IAA-phenylalanine (IAPhe), but not IAA-aspartate (IAAsp) as substrates. We also found a substantial amount of hydrolysis of an ester conjugate (IAA-glucose, IAGlu) in our enzyme preparation. The tentative reaction product IAA was identified by HPLC and subsequent GC-MS analysis. The pH optima for the different substrates were not identical, suggesting several hydrolase isoforms. After gel filtration chromatography we found at least two peaks containing different hydrolase isoforms. The isoform, which converted IAGlu to IAA, exhibited a molecular mass of ca 63 kDa, and an isoform of ca 21 kDa converted IAAla and IAPhe. The increased free IAA content in clubroot-diseased roots of Brassicaceae can be due to either de novo synthesis or release of IAA from conjugates. To answer this question free, ester- and amide-bound IAA was measured in 24- and 30-day-old leaves and roots of healthy and Plasmodiophora brassicae-infected Chinese cabbage, and the hydrolase activity with different substrates measured in the same tissues. The amide conjugates were dramatically enhanced in infected roots, whereas free IAA was only slightly enhanced compared to the control tissue. Hydrolase activity was also enhanced in clubbed roots, but the substrate specificity differed from that found in the seedlings. Especially, IAAsp hydrolysis was induced after inoculation with P. brassicae. We conclude that different auxin conjugates can be hydrolyzed at different developmental stages or under stress.
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element AMIDOHYDROIASE
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element ANXIN CONJUGATES
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element BRASSICACEAE
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element CHINESE CABBAGE
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element CLUBROOT DISEASE
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element INDOLE-3-ACETIC ACID
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element PLASMODIOPHORA BRASSICAE
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Ludwig‐Müller, J.
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Personal name Epstein, E.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Hilgenberg, W.
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/file/d/1CXW4eBBKHCUSEcUu7Q3jY0P7Y81044nn/view?usp=drive_link">https://drive.google.com/file/d/1CXW4eBBKHCUSEcUu7Q3jY0P7Y81044nn/view?usp=drive_link</a>
Public note Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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Source of classification or shelving scheme Clasificación local
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  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 26.06.2025   B-32 26.06.2025 26.06.2025 Documentos solicitados