|
type |
Journal Article |
authors |
Turner, S.R.; Ireland, R.; Rawsthorne, S. |
title |
Cloning and characterization of the P subunit of glycine decarboxylase from pea (Pisum sativum) |
journal |
J Biol Chem |
Activity |
1.4.4.2 |
Family |
1.4.4.2 |
sel |
selected |
ui |
1347530 |
year |
(1992) |
volume |
267 |
number |
8 |
pages |
5355-60 |
| |
abstract |
A pea leaf cDNA library constructed in lambda gt11 was screened with an antibody raised to the P subunit of glycine decarboxylase. One of the positive clones isolated was sequenced and shown to contain an open reading frame, which encoded the entire P subunit polypeptide. Aligning the deduced amino acid sequence with the amino acid sequence determined directly from the NH2 terminus of the mature P subunit shows the presence of a putative 86 amino acid leader sequence, presumably required for import into the mitochondria, and gives a Mr of the mature protein of 105,000. Comparison of this deduced amino acid sequence with the sequence of a pyridoxal phosphate-containing peptide isolated from the P subunit of chicken liver glycine decarboxylase shows remarkable conservation. The P subunit, however, shows little sequence homology with other published amino acid decarboxylases. Expression of the P subunit mRNA shows a pattern very similar to that of the corresponding polypeptide: it is strongly light induced and is expressed at a much higher level in leaves than in other tissues. Southern blot analysis suggests that the P subunit is encoded by a small multigene family. |
last changed |
2009/07/07 11:55 |
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