NDLI: Role of Tyr-435 of Vibrio harveyi Chitinase A in Chitin Utilization

Content Provider	Springer Nature Link
Author	Sritho, Natchak Suginta, Wipa
Copyright Year	2011
Abstract	Vibrio harveyi chitinase A or VhChiA (EC.3.2.1.14) is a member of GH-18 chitinases that catalyzes chitin degradation from marine biomaterials. Our earlier structural data of VhChiA suggested that Tyr-435 marks the ending of subsite +2 and may influence binding of the interacting substrate at the aglycone binding sites. This study reports the effects of Tyr-435 using site-directed mutagenesis technique. Mutation of Tyr-435 to Ala (mutant Y435A) enhanced both binding and catalytic efficiency of VhChiA, whereas substitution of Tyr-435 to Trp (mutant Y435W) lessened the ability of the enzyme to bind and hydrolyze chitin substrates. The increased activity of Y435A can be explained by partial removal of a steric clash around subsite (+2), thereby allowing a chitin chain to move beyond or to access the enzyme’s active site from the aglycone side more straightforwardly.
Starting Page	1192
Ending Page	1202
Page Count	11
File Format	PDF
ISSN	02732289
Journal	Applied Biochemistry and Biotechnology
Volume Number	166
Issue Number	5
e-ISSN	15590291
Language	English
Publisher	Humana Press Inc
Publisher Date	2011-12-23
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Chitin Chitinase Marine bacterium Site-directed mutagenesis Vibrio harveyi Biotechnology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Role of Tyr-435 of Vibrio harveyi chitinase A in chitin utilization.

Role of Chitin-Binding Proteins in the Specific Attachment of the Marine Bacterium Vibrio harveyi to Chitin

Functional analysis of active site residues of Bacillus thuringiensis WB7 chitinase by site-directed mutagenesis

Substrate binding modes and anomer selectivity of chitinase A from Vibrio harveyi

Chitin Degradation Proteins Produced by the Marine Bacterium Vibrio harveyi Growing on Different Forms of Chitin

Decolorization of Acid Black 210 by Vibrio harveyi TEMS1, a newly isolated bioluminescent bacterium from Izmir Bay, Turkey

Induction of Chitin-Binding Proteins during the Specific Attachment of the Marine Bacterium Vibrio harveyi to Chitin

The chitin-binding domain of a GH-18 chitinase from Vibrio harveyi is crucial for chitin-chitinase interactions.

Improving the Neutral Phytase Activity from Bacillus amyloliquefaciens DSM 1061 by Site-Directed Mutagenesis

Role of Tyr-435 of Vibrio harveyi Chitinase A in Chitin Utilization

Similar Documents

Role of Tyr-435 of Vibrio harveyi chitinase A in chitin utilization.

Role of Chitin-Binding Proteins in the Specific Attachment of the Marine Bacterium Vibrio harveyi to Chitin

Functional analysis of active site residues of Bacillus thuringiensis WB7 chitinase by site-directed mutagenesis

Substrate binding modes and anomer selectivity of chitinase A from Vibrio harveyi

Chitin Degradation Proteins Produced by the Marine Bacterium Vibrio harveyi Growing on Different Forms of Chitin

Decolorization of Acid Black 210 by Vibrio harveyi TEMS1, a newly isolated bioluminescent bacterium from Izmir Bay, Turkey

Induction of Chitin-Binding Proteins during the Specific Attachment of the Marine Bacterium Vibrio harveyi to Chitin

The chitin-binding domain of a GH-18 chitinase from Vibrio harveyi is crucial for chitin-chitinase interactions.

Improving the Neutral Phytase Activity from Bacillus amyloliquefaciens DSM 1061 by Site-Directed Mutagenesis

Role of Tyr-435 of Vibrio harveyi Chitinase A in Chitin Utilization