Hydroxycinnamic acid amide metabolism: physiology and biochemistry (Record no. 42905)

MARC details
000 -LEADER
fixed length control field 02401nam a2200193Ia 4500
003 - CONTROL NUMBER IDENTIFIER
control field MX-MdCICY
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20250625124723.0
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-8601
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 250602s9999 xx |||||s2 |||| ||und|d
245 10 - TITLE STATEMENT
Title Hydroxycinnamic acid amide metabolism: physiology and biochemistry
490 0# - SERIES STATEMENT
Volume/sequential designation Can. J. Bot., 80(6), p.577-589, 2002
520 3# - SUMMARY, ETC.
Summary, etc. Hydroxycinnamic acid amides (HCAAs)are a widely distributed group of plant secondary metabolites purported to function in several growth and developmental processes including floral induction, flower formation, sexual differentiation, tuberization, cell division, and cytomorphogenesis. Although most of these putative physiological roles for HCAAs remain controversial, the biosynthesis of amides and their subsequent olymerization in the plant cell wall are generally accepted as integral components of plant defense responses to pathogen challenge and wounding. Tyramine-derived HCAAs are commonly associated with the cell wall of tissues near pathogen-infected or woundhealing regions. Moreover, feruloyltyramine and feruloyloctapamine are covalent cell wall constituents of both natural and wound periderms of potato (Solanum tuberosum)tubers, and are putative components of the aromatic domain of suberin. The deposition of HCAAs is thought to create a barrier against pathogens by reducing cell wall digestibility. HCAAs are formed by the condensation of hydroxycinnamoyl-CoA thioesters with phenylethylamines such as tyramine, or polyamines such as putrescine. The ultimate step in tyramine-derived HCAA biosynthesis is catalyzed by hydroxycinnamoyl- CoA:tyramine N-(hydroxycinnamoyl)transferase (THT; E.C. 2.3.1.110). The enzyme has been isolated and purified from a variety of plants, and the corresponding cDNAs cloned from potato, tobacco (Nicotiana tabacum), and pepper (Capsicum annuum). THT exhibits homology with mammalian spermidine-spermine acetyltransferases and putative N-acetyltransferases from microorganisms. In this review, recent advances in our understanding of the physiology and biochemistry of HCAA biosynthesis in plants are discussed.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Facchini, P.J.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Hagel, J.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Zulak, K.G.
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/file/d/15EokCP9qOM_OCdSbAfvRujkJxpCf0nlw/view?usp=drivesdk">https://drive.google.com/file/d/15EokCP9qOM_OCdSbAfvRujkJxpCf0nlw/view?usp=drivesdk</a>
Public note Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Source of classification or shelving scheme Clasificación local
Koha item type Documentos solicitados
Holdings
Lost status Source of classification or shelving scheme Damaged status Not for loan Collection Home library Current library Shelving location Date acquired Total checkouts Full call number Date last seen Price effective from Koha item type
  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-8601 25.06.2025 25.06.2025 Documentos solicitados