|
type |
Journal Article |
authors |
Vaaler, G. L.; Brasch, M. A.; Snell, E. E. |
title |
Pyridoxal 5'-phosphate-dependent histidine decarboxylase. Nucleotide sequence of the hdc gene and the corresponding amino acid sequence |
journal |
J Biol Chem |
Activity |
4.1.1.22 |
Family |
4.1.1.22.a |
sel |
selected |
ui |
3015950 |
year |
(1986) |
volume |
261 |
number |
24 |
pages |
11010-4 |
| |
keywords |
Amino Acid Sequence |
abstract |
The nucleotide sequence of a 1.3-kilobase NaeI fragment from Morganella morganii AM-15 that contains the gene for histidine decarboxylase has been determined. The gene was initially identified among total chromosomal digests using a mixed sequence oligonucleotide probe corresponding to amino acids 11-16 of histidine decarboxylase and then cloned on a 5.5-kilobase PstI fragment. The structural gene contains 1131 nucleotides and encodes 377 amino acids with the sequence: (sequence: in text). The independently determined NH2-terminal sequence of this enzyme (Tanase, S., Guirard, B. M., and Snell, E. E. (1985) J. Biol. Chem. 260, 6738-6746) and the amino acid sequences of two tryptic peptides reported in the accompanying paper (Hayashi, H., Tanase, S., and Snell, E. E. (1986) J. Biol. Chem. 261, 11003-11009) are localized in the sequence presented here; the lysine that binds pyridoxal phosphate is situated at residue 232, whereas the serine that binds the adduct formed between pyridoxal phosphate and the inhibitor alpha- fluoromethylhistidine is positioned at residue 322. |
last changed |
2009/06/09 14:51 |
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