The N-terminal processing of MADH from the bacterium T versutus and the N-terminal heterogeneity of the isolated a subunit of the alpha2beta2 protein complex was demonstrated by a combination of... Show moreThe N-terminal processing of MADH from the bacterium T versutus and the N-terminal heterogeneity of the isolated a subunit of the alpha2beta2 protein complex was demonstrated by a combination of Edman sequence analysis of an electroblotted band, in situ digested with pyroglutamate aminopeptidase, and accurate mass determination of the homogenous subunit by the technique of electrospray ionisation mass spectrometry. From this study, it appears that the corresponding gene of the alpha subunit contains 395 amino acids and that it is preceded by a leader sequence of 31 residues. Show less
Huitema, F.; Beeumen, J. van; Driessche, G. van; Duine, J.A; Canters, G.W 1993
The gene that codes for the alpha-subunit of methylamine dehydrogenase from Thiobacillus versutus, madA, was cloned and sequenced. It codes for a protein of 395 amino acids preceded by a leader... Show moreThe gene that codes for the alpha-subunit of methylamine dehydrogenase from Thiobacillus versutus, madA, was cloned and sequenced. It codes for a protein of 395 amino acids preceded by a leader sequence of 31 amino acids. The derived amino acid sequence was confirmed by partial amino acid sequencing. The start of the mature protein could not be determined by direct sequencing, since the N terminus appeared to be blocked. Instead, it was determined by electrospray mass spectrometry. Confirmation of the results was obtained by sequencing the N terminus after pyroglutamate aminopeptidase, digestion. The sequence is homologous to the Paracoccus denitrificans nucleotide sequence. A second open reading frame, called open reading frame 3, is located immediately downstream of madA. Show less
