Precursor Structure of Cephalosporin Acylase: Insights into Auto-Proteolytic Activation in a New N-Terminal Hydrolase Family

Kim, Youngsoo; Kim, Sanggu; Earnest, Thomas N.; Hol, Wim G. J.

doi:10.1100/tsw.2002.54

Precursor Structure of Cephalosporin Acylase: Insights into Auto-Proteolytic Activation in a New N-Terminal Hydrolase Family

Journal Article · Tue Jan 01 00:00:00 EST 2002 · The Scientific World Journal (Online)

DOI:https://doi.org/10.1100/tsw.2002.54· OSTI ID:1629618

Kim, Youngsoo ^[1]; Kim, Sanggu ^[2]; Earnest, Thomas N. ^[3]; Hol, Wim G. J. ^[4]

Yeungnam Univ., Dae-Dong, Kyungsan (Korea, Republic of). School of Chemical Engineering; Univ. of Washington, Seattle, WA (United States). Biomolecular Structure Center. Dept. of Biochemistry; DOE/OSTI
Yeungnam Univ., Dae-Dong, Kyungsan (Korea, Republic of). School of Chemical Engineering
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Physical Biosciences Division. Berkeley Center for Structural Biology
Univ. of Washington, Seattle, WA (United States). Biomolecular Structure Center. Dept. of Biochemistry; Univ. of Washington, Seattle, WA (United States). Howard Hughes Medical Inst.

Autocatalytic proteolytic cleavage is a frequently observed post-translational modification in proteins. Cephalosporin acylase (CA) is a recently identified member of the Nterminal hydrolase family that is activated from an inactive precursor by autoproteolytic processing, generating a new N-terminal residue, which is either a Ser or a Thr[1]. The N-terminal Ser or Thr becomes a nucleophilic catalytic center for intramolecular and intermolecular amide cleavages. The gene structure of the open reading frame of CAs generally consist of a signal peptide followed by the α-subunit, a spacer sequence, and the β-subunit, which are all translated into a single polypeptide chain, the CA precursor. The precursor is post-translationally modified into an active heterodimeric enzyme with α- and β-subunits, first by intramolecular cleavage and second, by intermolecular cleavage.

Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1629618

Journal Information:: The Scientific World Journal (Online), Journal Name: The Scientific World Journal (Online) Vol. 2; ISSN 1537-744X

Publisher:: HindawiCopyright Statement

Country of Publication:: United States

Language:: English

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