ACPS Protein, Streptococcus pyogenes serotype M28 (Baculovirus, His-Myc)

ACPS Protein, Streptococcus pyogenes serotype M28 (Baculovirus, His-Myc), a 4-phosphopantetheinyl transferase, activates two distinct acyl carrier proteins (ACPs) that are present in fatty acid synthase (FAS) systems FAS-I and FAS-II, the ACP-I domain and the mycobacterial ACP-II protein (ACPM), respectively^[1].

Acyl carrier protein synthases (AcpSs), which are about 120 amino acid residues in length, and display a biologically active trimeric arrangement of α/β fold. A structure-based sequence comparison between AcpS and its ACP substrates from various species demonstrated that the proteins of the Corynebacterineae family display high sequence conservation, forming a segregated subgroup of AcpS and ACPs. Sequence-based structure analysis of AcpS and its ACP substrates from different species revealed that for the Corynebacterineae family of bacteria, AcpS, ACP-I, and ACPM each display high sequence conservation that sets them apart from other bacteria, fungi, and parasites^[1].

Others

Sf9 insect cells

N-10*His;C-Myc

Q48RM7 (M1-K118)

/

MIVGHGIDLQEISAIEKVYQRNPRFAQKILTEQELAIFESFPYKRRLSYLAGRWAGKEAFAKAIGTGIGRLTFQDIEILNDVRGCPILTKSPFKGNSFISISHSGNYVQASVILEDKK

Approximately 17.1 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.

• [1]. Orly Dym, et al. Structure-function analysis of the acyl carrier protein synthase (AcpS) from Mycobacterium tuberculosis. J Mol Biol. 2009 Nov 6;393(4):937-50.  [Content Brief]