|
type |
Journal Article |
authors |
Li, J.; Shah, S.; Moffatt, B. A.; Glick, B. R. |
title |
Isolation and characterization of an unusual 1-aminocyclopropane-1- carboxylic acid (ACC) deaminase gene from Enterobacter cloacae UW4 |
journal |
Antonie Van Leeuwenhoek |
Activity |
3.5.99.7 |
Family |
3.5.99.7 |
sel |
selected |
ui |
11827211 |
year |
(2001) |
volume |
80 |
number |
3-4 |
pages |
255-61 |
| |
keywords |
Amino Acid Sequence |
abstract |
A genomic library of the 1-aminocyclopropane-1-carboxylic acid (ACC) deaminase-containing plant growth-promoting bacterium Enterobacter cloacae UW4 in pUC19 in Escherichia coli was screened for the ability to utilize ACC as a sole source of nitrogen. One of the clones that was isolated contained a plasmid with an insert of approximately 0.8 kb that conferred ACC deaminase activity. Sequence analysis revealed that this DNA fragment contains an open-reading frame of 696 nucleotides predicted to encode a protein of 232 amino acids, a member of the amidohydrolase protein superfamily, i.e., a deaminase that contains a mononuclear or binuclear metal center as compared to the canonical ACC deaminase which contains pyridoxal phosphate as a co-factor. |
last changed |
2018/05/07 13:07 |
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