Enzymatic properties and deduced amino acid sequence of a high-alkaline pectate lyase from an alkaliphilic Bacillus isolate

1999 ◽  
Vol 1427 (2) ◽  
pp. 145-154 ◽  
Author(s):  
T Kobayashi
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Pectate Lyase ◽  
Enzymatic Properties ◽  
Alkaliphilic Bacillus ◽  
Alkaline Pectate Lyase ◽  
Bacillus Isolate

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

Enzymatic properties, crystallization, and deduced amino acid sequence of an alkaline endoglucanase from Bacillus circulans

2002 ◽  
Vol 1570 (3) ◽  
pp. 174-180 ◽  
Author(s):  
Yoshihiro Hakamada ◽  
Keiji Endo ◽  
Shuichi Takizawa ◽  
Tohru Kobayashi ◽  
Tsuyoshi Shirai ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Enzymatic Properties ◽  
Bacillus Circulans

Detection and sequence analysis of an altered pectate lyase gene in Pseudomonas syringae pv. glycinea and related bacteria

2006 ◽  
Vol 52 (11) ◽  
pp. 1051-1059 ◽  
Author(s):  
Ching-Hsing Liao ◽  
William Fett ◽  
Sean-Shong Tzean ◽  
Gabriel Hoffman
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Pseudomonas Syringae ◽  
Pectate Lyase ◽  
Site Directed Mutagenesis ◽  
Nucleotide Sequencing ◽  
Microbial Infection ◽  
Pectolytic Activity ◽  
Double Base ◽  
Base Insertion

Pectate lyase (PL) is a potent cell wall-degrading enzyme known to play a role in the microbial infection of plants. We re-examined the pectolytic property of seven representative pathovars of Pseudomonas syringae. None of the 10 P. syringae pv. glycinea strains examined exhibited pectolytic activity. However, the PL gene (pel) was detected by Southern hybridization in four out of four P. syringae pv. glycinea strains examined. A P. syringae pv. glycinea pel gene was cloned, sequenced, and predicted to encode a protein sharing 70%–90% identity in amino acid sequence with PLs produced by pectolytic pseudomonads and xanthomonads. A series of amino acid and nucleotide sequence analyses reveal that (i) the predicted P. syringae pv. glycinea PL contains two regions in the amino acid sequence that may affect the formation of a β-helix structure important for the enzyme activity, and (ii) the P. syringae pv. glycinea pel gene contains a single-base insertion, a double-base insertion, and an 18-bp deletion, which can lead to the synthesis of an inactive PL protein. The function of P. syringae pv. glycinea PL could be restored by removing the unwanted base insertions and by filling in the 18-bp deletions by site-directed mutagenesis. The altered pel sequence was also detected by polymerase chain reaction and nucleotide sequencing in the genomes of other pathovars of P. syringae, including phaseolicola and tagetis.Key words: pectate lyase, pel gene, Pseudomonas syringae, detection, analysis.

Deduced Amino Acid Sequence and Possible Catalytic Residues of a Thermostable, Alkaline Cellulase from an Alkaliphilic Bacillus Strain

2000 ◽  
Vol 64 (11) ◽  
pp. 2281-2289 ◽  
Author(s):  
Yoshihiro HAKAMADA ◽  
Yuji HATADA ◽  
Kenzo KOIKE ◽  
Tadashi YOSHIMATSU ◽  
Shuji KAWAI ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Catalytic Residues ◽  
Bacillus Strain ◽  
Alkaliphilic Bacillus ◽  
Alkaline Cellulase

scholarly journals Deduced amino-acid sequence and possible catalytic residues of a novel pectate lyase from an alkaliphilic strain of Bacillus

2000 ◽  
Vol 267 (8) ◽  
pp. 2268-2275 ◽  
Author(s):  
Yuji Hatada ◽  
Kazuhiro Saito ◽  
Kenzo Koike ◽  
Tadashi Yoshimatsu ◽  
Tadahiro Ozawa ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Pectate Lyase ◽  
Catalytic Residues
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