Ketimine reductase mu-crystallin (EC 1.5.1.25) (NADP-regulated thyroid-hormone-binding protein)
1_MSRVP 6_ AFLSA 11_ AEVEE 16_ HLRSS 21_ SLLIP 26_ PLETA 31_ LANFS 36_ SGPEG 41_ GVMQP 46_ VRTVV 51_ PVTKH 56_ RGYLG 61_ VMPAY 66_ SAAED 71_ ALTTK 76_ LVTFY 81_ EDRGI 86_ TSVVP 91_ SHQAT 96_ VLLFE 101_ PSNGT 106_ LLAVM 111_ DGNVI 116_ TAKRT 121_ AAVSA 126_ IATKF 131_ LKPPS 136_ SEVLC 141_ ILGAG 146_ VQAYS 151_ HYEIF 156_ TEQFS 161_ FKEVR 166_ IWNRT 171_ KENAE 176_ KFADT 181_ VQGEV 186_ RVCSS 191_ VQEAV 196_ AGADV 201_ IITVT 206_ LATEP 211_ ILFGE 216_ WVKPG 221_ AHINA 226_ VGASR 231_ PDWRE 236_ LDDEL 241_ MKEAV 246_ LYVDS 251_ QEAAL 256_ KESGD 261_ VLLSG 266_ AEIFA 271_ ELGEV 276_ IKGVK 281_ PAHCE 286_ KTTVF 291_ KSLGM 296_ AVEDT 301_ VAAKL 306_IYDSW
1: Catalyzes the NAD(P)H-dependent reduction of imine double bonds of a number of cyclic ketimine substrates, including sulfur-containing cyclic ketimines (PubMed:21332720, PubMed:25931162). Under physiological conditions, it efficiently catalyzes delta(1)-piperideine-2-carboxylate (P2C) and delta(1)-pyrroline-2-carboxylate (Pyr2C) reduction, suggesting a central role in lysine and glutamate metabolism (PubMed:25931162). Additional substrates are delta(2)-thiazoline-2-carboxylate (T2C), 3,4-dehydrothiomorpholine-3-carboxylate (AECK), and (R)-lanthionine ketimine (LK) that is reduced at very low rate compared to other substrates (PubMed:25931162). Also catalyzes the NAD(P)H-dependent reduction of (S)-cystathionine ketimine (CysK) (By similarity)