5loa: Difference between revisions
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==Crystal structure of the engineered D-Amino Acid Dehydrogenase (DAADH) bound to NADP+== | ==Crystal structure of the engineered D-Amino Acid Dehydrogenase (DAADH) bound to NADP+== | ||
<StructureSection load='5loa' size='340' side='right' caption='[[5loa]], [[Resolution|resolution]] 1.84Å' scene=''> | <StructureSection load='5loa' size='340' side='right'caption='[[5loa]], [[Resolution|resolution]] 1.84Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5loa]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Corgl Corgl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LOA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LOA FirstGlance]. <br> | <table><tr><td colspan='2'>[[5loa]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Corgl Corgl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LOA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LOA FirstGlance]. <br> | ||
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[[Category: Corgl]] | [[Category: Corgl]] | ||
[[Category: Diaminopimelate dehydrogenase]] | [[Category: Diaminopimelate dehydrogenase]] | ||
[[Category: Large Structures]] | |||
[[Category: Dunstan, M S]] | [[Category: Dunstan, M S]] | ||
[[Category: Gahloth, D]] | [[Category: Gahloth, D]] | ||
Revision as of 09:30, 16 October 2019
Crystal structure of the engineered D-Amino Acid Dehydrogenase (DAADH) bound to NADP+Crystal structure of the engineered D-Amino Acid Dehydrogenase (DAADH) bound to NADP+
Structural highlights
Function[DAPDH_CORGL] Catalyzes the reversible NADPH-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. Probably plays a role in lysine biosynthesis. Exhibits a high substrate specificity for meso-2,6-diaminopimelate, since L,L-2,6-diaminopimelate, D,D-2,6-diaminopimelate, L-glutamate, L-alanine, L-leucine, L-valine, L-aspartate, L-threonine, L-homoserine, L-methionine, L-lysine, L-serine, L-phenylalanine, L-tyrosine, L-tryptophan, L-ornithine, L-histidine, L-arginine, D-glutamate, and D-alanine are not substrates for the oxidative deamination reaction. Can use NAD(+) only poorly since the activity observed in the presence of NAD(+) is about 3% of that with NADP(+).[1] [2] References
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