|
|
|
|
| LEADER |
01000caa a22002652 4500 |
| 001 |
NLM117437913 |
| 003 |
DE-627 |
| 005 |
20250203032343.0 |
| 007 |
tu |
| 008 |
231222s2000 xx ||||| 00| ||eng c |
| 028 |
5 |
2 |
|a pubmed25n0392.xml
|
| 035 |
|
|
|a (DE-627)NLM117437913
|
| 035 |
|
|
|a (NLM)11858251
|
| 040 |
|
|
|a DE-627
|b ger
|c DE-627
|e rakwb
|
| 041 |
|
|
|a eng
|
| 100 |
1 |
|
|a Bernards, M A
|e verfasserin
|4 aut
|
| 245 |
1 |
0 |
|a Induced phenylpropanoid metabolism during suberization and lignification
|b a comparative analysis
|
| 264 |
|
1 |
|c 2000
|
| 336 |
|
|
|a Text
|b txt
|2 rdacontent
|
| 337 |
|
|
|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
|
| 338 |
|
|
|a Band
|b nc
|2 rdacarrier
|
| 500 |
|
|
|a Date Completed 07.05.2002
|
| 500 |
|
|
|a Date Revised 30.09.2020
|
| 500 |
|
|
|a published: Print
|
| 500 |
|
|
|a Citation Status MEDLINE
|
| 520 |
|
|
|a Induction of the biosynthesis of phenylpropanoids was monitored at the enzyme level through measurement of the temporal change in the activity of two marker enzymes of phenylpropanoid metabolism, phenylalanine ammonia-lyase, (PAL, E.C. 4.1.3.5) and 4-coumaryl-CoA ligase (4-CL, E.C. 6.2.1.12) and two marker enzymes for hydroxycinnamyl alcohol biosynthesis, cinnamoyl-CoA:NADP+ oxidoreductase (CCR, E.C. 1.2.1.44) and cinnamyl alcohol dehydrogenase (CAD, E.C. 1.1.1.195) in both suberizing potato (Solanum tuberosum) tubers and lignifying loblolly pine (Pinus taeda) cell cultures. While measurable activities of PAL, 4-CL and CAD increased upon initiation of suberization in potato tubers, that of CCR did not. By contrast, all four enzymes were induced upon initiation of lignification in pine cell cultures. The lack of CCR induction in potato by wound treatment is consistent with the channelling of hydroxycinnamoyl-CoA derivatives away from monolignol formation and toward other hydroxycinnamoyl derivatives such as those that accumulate during suberization
|
| 650 |
|
4 |
|a Journal Article
|
| 650 |
|
4 |
|a Research Support, Non-U.S. Gov't
|
| 650 |
|
4 |
|a Research Support, U.S. Gov't, Non-P.H.S.
|
| 650 |
|
4 |
|a NASA Discipline Plant Biology
|
| 650 |
|
4 |
|a Non-NASA Center
|
| 650 |
|
7 |
|a Coumaric Acids
|2 NLM
|
| 650 |
|
7 |
|a Lipids
|2 NLM
|
| 650 |
|
7 |
|a Membrane Lipids
|2 NLM
|
| 650 |
|
7 |
|a suberin
|2 NLM
|
| 650 |
|
7 |
|a 8072-95-5
|2 NLM
|
| 650 |
|
7 |
|a Lignin
|2 NLM
|
| 650 |
|
7 |
|a 9005-53-2
|2 NLM
|
| 650 |
|
7 |
|a Alcohol Oxidoreductases
|2 NLM
|
| 650 |
|
7 |
|a EC 1.1.-
|2 NLM
|
| 650 |
|
7 |
|a cinnamyl alcohol dehydrogenase
|2 NLM
|
| 650 |
|
7 |
|a EC 1.1.1.195
|2 NLM
|
| 650 |
|
7 |
|a Aldehyde Oxidoreductases
|2 NLM
|
| 650 |
|
7 |
|a EC 1.2.-
|2 NLM
|
| 650 |
|
7 |
|a cinnamoyl CoA reductase
|2 NLM
|
| 650 |
|
7 |
|a EC 1.2.1.44
|2 NLM
|
| 650 |
|
7 |
|a Phenylalanine Ammonia-Lyase
|2 NLM
|
| 650 |
|
7 |
|a EC 4.3.1.24
|2 NLM
|
| 650 |
|
7 |
|a Coenzyme A Ligases
|2 NLM
|
| 650 |
|
7 |
|a EC 6.2.1.-
|2 NLM
|
| 650 |
|
7 |
|a 4-coumarate-CoA ligase
|2 NLM
|
| 650 |
|
7 |
|a EC 6.2.1.12
|2 NLM
|
| 700 |
1 |
|
|a Susag, L M
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Bedgar, D L
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Anterola, A M
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Lewis, N G
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Lewis, N G
|e investigator
|4 oth
|
| 773 |
0 |
8 |
|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 157(2000), 6 vom: 31. Dez., Seite 601-7
|w (DE-627)NLM098174622
|x 0176-1617
|7 nnns
|
| 773 |
1 |
8 |
|g volume:157
|g year:2000
|g number:6
|g day:31
|g month:12
|g pages:601-7
|
| 912 |
|
|
|a GBV_USEFLAG_A
|
| 912 |
|
|
|a SYSFLAG_A
|
| 912 |
|
|
|a GBV_NLM
|
| 912 |
|
|
|a GBV_ILN_350
|
| 951 |
|
|
|a AR
|
| 952 |
|
|
|d 157
|j 2000
|e 6
|b 31
|c 12
|h 601-7
|