J. Biochem, 1992, Vol. 112, No. 6 737-742
© 1992 Japanese Biochemical Society
The Primary Structure of Porcine Aminoacylase 1 Deduced from cDNA Sequence1
Masanori Mitta*,
Hiroshi Ohnogi**,
Akira Yamamoto**,
Ikunoshin Kato*,
Fumio Sakiyama** and
Susumu Tsunasawa*,2
*Biotechnology Research Laboratories, Takara Shuzo Co., Ltd. Seta, Otsu 520
**Institute for Protein Research, Osaka University Suita, Osaka 565
2To whom correspondence should be addressed
A cDNA encoding the complete amino acid sequence of aminoacylase 1 (N-acylamino acid aminohydrolase, ACY-1) [EC 3.5.1.14], a dimeric metalloprotein having two Zn2+ in the molecule, which catalyzes the deacylation of N-acylated L-amino acids except L-aspartic acid, has been isolated from porcine kidney 
gt10 cDNA library and sequenced. From sequence analysis of the cDNA and the N- and C-terminal amino acid analyses of the purified protein, it is deduced that porcine kidney ACY-1 consists of two identical subunits (Mr 45,260), each of which consists of a single chain of 406 amino acids with acetylalanine at the N-terminus. A cDNA encoding porcine liver ACY-1 was also cloned. The amino acid sequence deduced from the nucleotide sequence of the cDNA from porcine liver was identical to that deduced for porcine kidney ACY-1. Northern blot analysis suggested that ACY-1 is more highly expressed in kidney than in liver. Comparison of the amino acid sequence of porcine ACY-1 with those of other Zn2+-binding metalloenzymes showed no significant homologies in either the overall sequence or the consensus sequences for the metal binding sites. This indicates that ACY-1 is a new type of metalloprotein.
1 This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.
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