Acyl-coenzyme A thioesterase MBLAC2 (Acyl-CoA thioesterase MBLAC2) (EC 3.1.2.2) (Beta-lactamase MBLAC2) (EC 3.5.2.6) (Metallo-beta-lactamase domain-containing protein 2) (Palmitoyl-coenzyme A thioesterase MBLAC2)
1_MSALE 6_ WYAHK 11_ SLGDG 16_ IFWIQ 21_ ERFYE 26_ SGNRA 31_ NIWLV 36_ RGSEQ 41_ DVVID 46_ TGLGL 51_ RSLPE 56_ YLYSS 61_ GLLQD 66_ REAKE 71_ DAARR 76_ PLLAV 81_ ATHVH 86_ FDHSG 91_ GLYQF 96_ DRVAV 101_ HHAEA 106_ EALAR 111_ GDNFE 116_ TVTWL 121_ SDSEV 126_ VRTPS 131_ PGWRA 136_ RQFRV 141_ QAVQP 146_ TLILQ 151_ DGDVI 156_ NLGDR 161_ QLTVM 166_ HMPGH 171_ SRGSI 176_ CLHDK 181_ DRKIL 186_ FSGDV 191_ VYDGS 196_ LIDWL 201_ PYSRI 206_ SDYVG 211_ TCERL 216_ IELVD 221_ RGLVE 226_ KVLPG 231_ HFNTF 236_ GAERL 241_ FRLAS 246_ NYISK 251_ AGICH 256_ KVSTF 261_ AMRSL 266_ ASLAL 271_RVTNS
1: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH (PubMed:33219126). Has an acyl-CoA thioesterase activity towards the long chain fatty acyl-CoA thioester palmitoyl-CoA (hexadecanoyl-CoA; C16:0-CoA) (PubMed:33219126). Displays a substrate preference for fatty acyl-CoAs with chain-lengths C12-C18 (PubMed:33219126). Possesses beta-lactamase activity, catalyzing the hydrolysis of penicillin G and nitrocefin (PubMed:31434986). Exhibits no activity towards other beta-lactam antibiotic classes including cephalosporins (cefotaxime) and carbapenems (imipenem) (PubMed:31434986)