Highly alkaline pectate lyase Pel-4A from alkaliphilic Bacillus sp. strain P-4-N: its catalytic properties and deduced amino acid sequence

Extremophiles ◽  
2000 ◽  
Vol 4 (6) ◽  
pp. 377-383 ◽  
Author(s):  
Tohru Kobayashi ◽  
Yuji Hatada ◽  
Atsushi Suzumatsu ◽  
Katsuhisa Saeki ◽  
Yoshihiro Hakamada ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Catalytic Properties ◽  
Pectate Lyase ◽  
Bacillus Sp ◽  
Alkaliphilic Bacillus ◽  
Alkaline Pectate Lyase

scholarly journals Partial amino acid sequence of protease I produced by Bacillus sp. 11-4 isolated from Vietnamese fish sauces

2003 ◽  
Vol 29 (1) ◽  
pp. 25-31 ◽  
Author(s):  
Yoshitaka NISHIYAMA ◽  
Haruko MAEDA ◽  
Toshio NAGASHIMA ◽  
Toshihiro WATANABE ◽  
Kiyoshi MURA
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Bacillus Sp ◽  
Partial Amino Acid Sequence

scholarly journals Cholest-4-En-3-One-Δ1-Dehydrogenase, a Flavoprotein Catalyzing the Second Step in Anoxic Cholesterol Metabolism

2007 ◽  
Vol 74 (1) ◽  
pp. 107-113 ◽  
Author(s):  
Yin-Ru Chiang ◽  
Wael Ismail ◽  
Sébastien Gallien ◽  
Dimitri Heintz ◽  
Alain Van Dorsselaer ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Sequence Identity ◽  
Catalytic Properties ◽  
Cholesterol Metabolism ◽  
Catalytic Efficiency ◽  
Second Step ◽  
Terminal Amino Acid ◽  
Competitive Inhibitors ◽  
Terminal Amino

ABSTRACT The anoxic metabolism of cholesterol was studied in the denitrifying bacterium Sterolibacterium denitrificans, which was grown with cholesterol and nitrate. Cholest-4-en-3-one was identified before as the product of cholesterol dehydrogenase/isomerase, the first enzyme of the pathway. The postulated second enzyme, cholest-4-en-3-one-Δ1-dehydrogenase, was partially purified, and its N-terminal amino acid sequence and tryptic peptide sequences were determined. Based on this information, the corresponding gene was amplified and cloned and the His-tagged recombinant protein was overproduced, purified, and characterized. The recombinant enzyme catalyzes the expected Δ1-desaturation (cholest-4-en-3-one to cholesta-1,4-dien-3-one) under anoxic conditions. It contains approximately one molecule of FAD per 62-kDa subunit and forms high molecular aggregates in the absence of detergents. The enzyme accepts various artificial electron acceptors, including dichlorophenol indophenol and methylene blue. It oxidizes not only cholest-4-en-3-one, but also progesterone (with highest catalytic efficiency, androst-4-en-3,17-dione, testosterone, 19-nortestosterone, and cholest-5-en-3-one. Two steroids, corticosterone and estrone, act as competitive inhibitors. The dehydrogenase resembles 3-ketosteroid-Δ1-dehydrogenases from other organisms (highest amino acid sequence identity with that from Pseudoalteromonas haloplanktis), with some interesting differences. Due to its catalytic properties, the enzyme may be useful in steroid transformations.

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