Experimental evidence for structure-activity features in common between mammalian histidine decarboxylase and ornithine decarboxylase
Keyword(s):
Common protein motifs between histidine decarboxylase (HDC) and ornithine decarboxylase (ODC) were detected by computational analysis. Mutants were generated and expressed in vitro. In both enzymes, terminal PEST-region-containing fragments are not essential for decarboxylation (PEST regions are sequence fragments enriched in proline, glutamic acid, serine and threonine residues in a hydrophilic fragment flanked by cationic amino acids). The substitution of a very well conserved histidine residue by alanine causes a severalfold increase of the apparent Km values for the respective substrates.
2010 ◽
Vol 53
(5)
◽
pp. 1990-1999
◽
1997 ◽
Vol 272
(4)
◽
pp. R1060-R1068
◽
Keyword(s):
1992 ◽
Vol 12
(5)
◽
pp. 2178-2185
◽
Keyword(s):
2010 ◽
Vol 53
(24)
◽
pp. 8619-8626
◽
1984 ◽
Vol 30
(2)
◽
pp. 236-246
◽
Keyword(s):
1994 ◽
Vol 59
(6)
◽
pp. 1430-1438
◽
Keyword(s):
1992 ◽
Vol 12
(5)
◽
pp. 2178-2185
Keyword(s):