1985
DOI: 10.1007/bf02418236
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Isolation and characterization of a gene encoding meso-diaminopimelate dehydrogenase fromGlycine max

Abstract: A detailed characterization of the lysine biosynthetic pathway in plants is yet to be completed. It is, however, assumed that the diaminopimelic acid pathway exists in the plant kingdom, as commonly described forEscherichia coli.Modification and refinement of lytic complementation, a technique previously utilized in bacterial systems, facilitated the isolation of a functional Diaminopimelate Dehydrogenase gene from aGlycine max nuclear gene library. The isolated gene codes for the enzyme meso-diaminopimelate d… Show more

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Cited by 23 publications
(15 citation statements)
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“…There are other examples in which cloned animal or plant genes have been shown to complement bacterial mutations (31)(32)(33)(34)(35)(36)(37)(38). These examples indicate the feasibility of cloning genes from higher eukaryotes by passing expression libraries through bacterial mutants and selecting for complementation.…”
Section: Discussionmentioning
confidence: 99%
“…There are other examples in which cloned animal or plant genes have been shown to complement bacterial mutations (31)(32)(33)(34)(35)(36)(37)(38). These examples indicate the feasibility of cloning genes from higher eukaryotes by passing expression libraries through bacterial mutants and selecting for complementation.…”
Section: Discussionmentioning
confidence: 99%
“…The most-known D-AADH is meso-diaminopimelate dehydrogenase (meso-DAPDH; EC 1.4.1.16), which is a key enzyme in the lysine biosynthetic pathway and has been found in bacteria, such as Bacillus sphaericus (17) and Corynebacterium glutamicum (14). In addition, meso-DAPDH has also been isolated from plants, for example, soybeans (Glycine max) (24). meso-DAPDH is NADP ϩ dependent and catalyzes the reversible oxidative deamination on the D-configuration center of meso-2,6-diaminopimelate (meso-DAP) to yield L-2-amino-6-oxopimelate (17).…”
mentioning
confidence: 99%
“…One unit of enzyme is defined as the amount that catalyses an increase of absorbance of 0.001 OD/min, after attaining maximum velocity. Dihydrodipicolinate reductase (EC 1.3.1.3 C) was measured by the oxidation of N A D P H using a reaction mixture similar to that of Farkas and Gilvarg [25] employing synthetic dihydrodipicolinate. The activity of this enzyme was verified by its susceptibility to inhibition with dipicolinic acid, a known inhibitor of the reductase.…”
Section: Enzyme Assaysmentioning
confidence: 99%
“…This enzyme would be characteristic of the long version of the standard pathway. However, Wenko et al [25] report m-DAP dehydrogenase to be a component of soybean (Glycine max), which would favor the shortened biosynthesis.…”
Section: Introductionmentioning
confidence: 99%