Enzymatic properties of the highly thermophilic and alkaline pectate lyase Pel-4B from alkaliphilic Bacillus sp. strain P-4-N and the entire nucleotide and amino acid sequences

Extremophiles ◽  
2001 ◽  
Vol 5 (2) ◽  
pp. 127-133 ◽  
Author(s):  
Yuji Hatada ◽  
Tohru Kobayashi ◽  
Susumu Ito
Keyword(s):  
Amino Acid ◽  
Pectate Lyase ◽  
Amino Acid Sequences ◽  
Enzymatic Properties ◽  
Bacillus Sp ◽  
Alkaliphilic Bacillus ◽  
Alkaline Pectate Lyase

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 and Nucleotide and Amino Acid Sequences of a Thermostable β-Agarase from the Novel Marine Isolate, JAMB-A94

2004 ◽  
Vol 68 (5) ◽  
pp. 1073-1081 ◽  
Author(s):  
Yukari OHTA ◽  
Yuichi NOGI ◽  
Masayuki MIYAZAKI ◽  
Zhijun LI ◽  
Yuji HATADA ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Enzymatic Properties ◽  
The Novel ◽  
Marine Isolate

scholarly journals Two Highly Similar Chitinases from Marine Vibrio Species have Different Enzymatic Properties

Marine Drugs ◽  
2020 ◽  
Vol 18 (3) ◽  
pp. 139
Author(s):  
Xinxin He ◽  
Min Yu ◽  
Yanhong Wu ◽  
Lingman Ran ◽  
Weizhi Liu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Extracellular Enzymes ◽  
Vibrio Harveyi ◽  
Amino Acid Sequences ◽  
Enzymatic Properties ◽  
Site Directed Mutagenesis ◽  
Amino Acid Residues ◽  
Marine Vibrio ◽  
Key Sites

Chitinase, as one of the most important extracellular enzymes in the marine environment, has great ecological and applied values. In this study, two chitinases (Chi1557 and Chi4668) with 97.33% amino acid sequences identity were individually found in Vibrio rotiferianus and Vibrio harveyi. They both were encoding by 561 amino acids, but differed in 15 amino acids and showed different enzymatic properties. The optimal temperature and pH ranges were 45–50 °C and pH 5.0–7.0 for Chi1557, while ~50 °C and pH 3.0–6.0 for Chi4668. K+, Mg2+, and EDTA increased the enzymatic activity of Chi4668 significantly, yet these factors were inhibitory to Chi1557. Moreover, Chi1557 degraded colloidal chitin to produce (GlcNAc)2 and minor GlcNAc, whereas Chi4668 produce (GlcNAc)2 with minor (GlcNAc)3 and (GlcNAc)4. The Kcat/Km of Chi4668 was ~4.7 times higher than that of Chi1557, indicating that Chi4668 had stronger catalytic activity than Chi1557. Furthermore, site-directed mutagenesis was performed on Chi1557 focusing on seven conserved amino acid residues of family GH18 chitinases. Chi1557 was almost completely inactive after Glu154, Gln219, Tyr221, or Trp312 was individually mutated, retained ~50% activity after Tyr37 was mutated, and increased two times activity after Asp152 was mutated, indicating that these six amino acids were key sites for Chi1557.

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