N-acetylneuraminate lyase (NALase) (EC 4.1.3.3) (N-acetylneuraminate pyruvate-lyase) (N-acetylneuraminic acid aldolase) (Sialate lyase) (Sialate-pyruvate lyase) (Sialic acid aldolase) (Sialic acid lyase)
1_MAFPK 6_ KKLQG 11_ LVAAT 16_ ITPMT 21_ ENGEI 26_ NFSVI 31_ GQYVD 36_ YLVKE 41_ QGVKN 46_ IFVNG 51_ TTGEG 56_ LSLSV 61_ SERRQ 66_ VAEEW 71_ VTKGK 76_ DKLDQ 81_ VIIHV 86_ GALSL 91_ KESQE 96_ LAQHA 101_ AEIGA 106_ DGIAV 111_ IAPFF 116_ LKPWT 121_ KDILI 126_ NFLKE 131_ VAAAA 136_ PALPF 141_ YYYHI 146_ PALTG 151_ VKIRA 156_ EELLD 161_ GILDK 166_ IPTFQ 171_ GLKFS 176_ DTDLL 181_ DFGQC 186_ VDQNR 191_ QQQFA 196_ FLFGV 201_ DEQLL 206_ SALVM 211_ GATGA 216_ VGSTY 221_ NYLGK 226_ KTNQM 231_ LEAFE 236_ QKDFS 241_ LALNY 246_ QFCIQ 251_ RFINF 256_ VVKLG 261_ FGVSQ 266_ TKAIM 271_ TLVSG 276_ IPMGP 281_ PRLPL 286_ QKASR 291_ EFTDS 296_ AEAKL 301_ KSLDF 306_ LSFTD 311_LKDGN
1: Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate (PubMed:33895133). It prevents sialic acids from being recycled and returning to the cell surface (PubMed:33895133). Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway (PubMed:22692205, PubMed:33895133). Although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded (Probable)