{'fraction_non_alphanumeric': 0.03741746148202495, 'fraction_numerical': 0.022743947175348497, 'mean_word_length': 4.982456140350878, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 1, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Human mitochondrial propionyl-CoA carboxylase: localization of the N-terminus of the pro- and mature alpha chains in the deduced primary sequence of a full-length cDNA.

Propionyl-CoA carboxylase [E.C.6.4.1.3] is a mitochondrial enzyme consisting of a and 0 polypeptides. Inherited deficiency of the enzyme activity leads to propionicacidemia. To further investigate the mutations involved in this metabolic disorder, we have previously cloned partial cDNAs to both subunits (1). We now report a full-length, 2478 nucleotide cDNA (pPCCA32) coding for the a, biotin-containing polypeptide. It contains a 5-untranslated sequence of 48 nucleotides, an open reading frame of 2106 nucleotides coding for a 702 amino acid pre-a polypeptide with the biotin-binding site at residue 668 (bold in figure) and a 3-untranslated sequence of 246 nucleotides with the consensus polyadenylation AATAAA (underlined) upstream of a poly(A) tail. A match of twenty-eight amnino acids (underlined) with the N-terminal amino acid sequence determined from the mature a polypeptide of purified human liver enzyme, separated from the polypeptide by HPLC, was found in the deduced sequence of the cDNA. Two methionine residues (in bold) are located in the putative mitochondrial leader sequence of 26 amino acids. As typical of such sequences, this region is hydrophobic and arginine rich.