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Probably plays a role in lysine biosynthesis. Exhibits a high substrate specificity, since alpha-ketoglutarate, pyruvate, oxaloacetate, glyoxylate, alpha-ketobutyrate, alpha-ketovalerate, alpha-ketocaproate, alpha-ketoisocaproate, alpha-ketoisovalerate, and phenylpyruvate are not substrates for the reductive amination reaction, and L,L-2,6-diaminopimelate, D,D-2,6-diaminopimelate, DL-alpha-aminopimelate, meso- and DL-2,5-diaminoadipate, L-djenkolate, L-cystine, L-lysine, S-(beta-aminoethy1)-L-homocysteine, L-ornithine, L-arginine, L-alpha,gamma-diaminobutyrate, L-histidine, L-phenylalanine, L-tyrosine, L-glutamate, L-aspartate, L-leucine, L-valine, L-methionine, L-serine, L-alanine, L-alpha-aminobutyrate, D-lysine, D-glutamate, D-leucine, D-alanine, D-phenylalanine, epsilon-aminocaproate, 7-aminoheptanoate, and 8-aminooctanoate are not substrates for the oxidative deamination reaction. Cannot use NAD(+) or NAD(+) analogs instead of NADP(+) for the oxidative deamination reaction"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"meso-2,6-diaminopimelate + NADP(+) + H2O = (S)-2-amino-6-oxoheptanedioate + NH4(+) + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13561"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:57791"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:58556"}],"ecNumber":"1.4.1.16","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7430138"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"762012"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7430138"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.4"}],"value":"L,L-2,6-diaminopimelate, D,D-2,6-diaminopimelate and meso-2,5-diaminoadipate competitively inhibit the oxidation of meso-2,6-diaminopimelate. L-2-amino-6-methylene-pimelate is also a potent competitive inhibitor (5 uM) of this reaction. Glyoxylate inhibits the reductive amination of L-2-amino-6-oxopimelate about 30%. The enzyme is inhibited completely by p-chloromercuribenzoate and HgCl(2) in vitro"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":2.5,"unit":"mM","substrate":"meso-2,6-diaminoheptanedioate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7430138"}]},{"constant":83.0,"unit":"uM","substrate":"NADP(+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7430138"}]},{"constant":0.2,"unit":"mM","substrate":"NADPH","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7430138"}]},{"constant":0.24,"unit":"mM","substrate":"L-2-amino-6-oxoheptanedioate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7430138"}]},{"constant":12.5,"unit":"mM","substrate":"ammonia","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7430138"}]}],"note":{"texts":[{"value":"The rate of the reductive amination reaction is about 11 times higher than that of the oxidative deamination at pH 7.5."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7430138"}],"value":"Optimum pH is about 10.5 for the oxidative deamination of meso-diaminopimelate and 7.5 for the reductive amination of L-2-amino-6-oxopimelate. The rate of the amination reaction declines markedly above pH 9.0."}]}},{"texts":[{"value":"Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7430138"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"762012"}],"value":"Constitutively expressed. Not induced by meso-2,6-diaminopimelate"}],"commentType":"INDUCTION"},{"texts":[{"value":"The reductive amination proceeds through a sequential ordered ternary-binary mechanism. NADPH binds first to the enzyme followed by L-2-amino-6-ketopimelate and ammonia, and the products are released in the order of meso-2,6-diaminopimelate and NADP(+). 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