NDLI: Catalytic Mechanism of S-type Phycobiliprotein Lyase CHAPERONE-LIKE ACTION AND FUNCTIONAL AMINO ACID RESIDUES

Content Provider	Journal of Biological Chemistry (JBC)
Author	Kupka, Michaela Zhang, Juan Fu, Wei-Lei Tu, Jun-Ming Böhm, Stephan Su, Ping Chen, Yu Zhou, Ming Scheer, Hugo Zhao, Kai-Hong
Abstract	The phycobilin:cysteine 84-phycobiliprotein lyase, CpcS1, catalyzes phycocyanobilin (PCB) and phycoerythrobilin (PEB) attachment at nearly all cysteine 82 binding sites (consensus numbering) of phycoerythrin, phycoerythrocyanin, phycocyanin, and allophycocyanin (Zhao, K. H., Su, P., Tu, J. M., Wang, X., Liu, H., Plöscher, M., Eichacker, L., Yang, B., Zhou, M., and Scheer, H. (2007) Proc. Natl. Acad. Sci. U.S.A. 104, 14300–14305). We now show that CpcS1 binds PCB and PEB rapidly with bi-exponential kinetics (38/119 and 12/8300 ms, respectively). Chromophore binding to the lyase is reversible and much faster than the spontaneous, but low fidelity chromophore addition to the apo-protein in the absence of the lyase. This indicates kinetic control by the enzyme, which then transfers the chromophore to the apo-protein in a slow (tens of minutes) but stereo- and regioselectively corrects the reaction. This mode of action is reminiscent of chaperones but does not require ATP. The amino acid residues Arg-18 and Arg-149 of the lyase are essential for chromophore attachment in vitro and in Escherichia coli, mutations of His-21, His-22, Trp-75, Trp-140, and Arg-147 result in reduced activity (<30% of wild type in vitro). Mutants R147Q and W69M were active but had reduced capacity for PCB binding; additionally, with W69M there was loss of fidelity in chromophore attachment. Imidazole is a non-competitive inhibitor, supporting a bilin-binding function of histidine. Evidence was obtained that CpcS1 also catalyzes exchange of C-β84-bound PCB in biliproteins by PEB.
Related Links	http://www.jbc.org/content/284/52/36405.abstract
Ending Page	36414
Starting Page	36405
Page Count	10
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	52
Volume Number	284
DOI	10.1074/jbc.M109.056382
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2009-12-25
Access Restriction	Open
Subject Keyword	Enzyme Catalysis and Regulation
Alternative Title	Catalytic Mechanism of S-type Phycobiliprotein Lyase
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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

Catalytic mechanism of S-type phycobiliprotein lyase: chaperone-like action and functional amino acid residues.

Catalytic Mechanism of S-type Phycobiliprotein Lyase

Sulfur Mobilization in Cyanobacteria THE CATALYTIC MECHANISM OF L-CYSTINE C-S LYASE (C-DES) FROM SYNECHOCYSTIS

Identification of a Mouse Short-chain Dehydrogenase/Reductase Gene, Retinol Dehydrogenase-similar FUNCTION OF NON-CATALYTIC AMINO ACID RESIDUES IN ENZYME ACTIVITY

Insights into the Catalytic Mechanism of Tyrosine Phenol-lyase from X-ray Structures of Quinonoid Intermediates

Key Role of Amino Acid Residues in the Dimerization and Catalytic Activation of the Autolysin LytA, an Important Virulence Factor in Streptococcus pneumoniae

Identification of Acid-Base Catalytic Residues of High-Mr Thioredoxin Reductase from Plasmodium falciparum

Regulation of the Catalytic Activity and Structure of Human Thioredoxin 1 via Oxidation and S-Nitrosylation of Cysteine Residues

Structure and Catalytic Mechanism of Yeast 4-Amino-4-deoxychorismate Lyase

Catalytic Mechanism of S-type Phycobiliprotein Lyase CHAPERONE-LIKE ACTION AND FUNCTIONAL AMINO ACID RESIDUES

Similar Documents

Catalytic mechanism of S-type phycobiliprotein lyase: chaperone-like action and functional amino acid residues.

Catalytic Mechanism of S-type Phycobiliprotein Lyase

Sulfur Mobilization in Cyanobacteria THE CATALYTIC MECHANISM OF L-CYSTINE C-S LYASE (C-DES) FROM SYNECHOCYSTIS

Identification of a Mouse Short-chain Dehydrogenase/Reductase Gene, Retinol Dehydrogenase-similar FUNCTION OF NON-CATALYTIC AMINO ACID RESIDUES IN ENZYME ACTIVITY

Insights into the Catalytic Mechanism of Tyrosine Phenol-lyase from X-ray Structures of Quinonoid Intermediates

Key Role of Amino Acid Residues in the Dimerization and Catalytic Activation of the Autolysin LytA, an Important Virulence Factor in Streptococcus pneumoniae

Identification of Acid-Base Catalytic Residues of High-Mr Thioredoxin Reductase from Plasmodium falciparum

Regulation of the Catalytic Activity and Structure of Human Thioredoxin 1 via Oxidation and S-Nitrosylation of Cysteine Residues

Structure and Catalytic Mechanism of Yeast 4-Amino-4-deoxychorismate Lyase

Catalytic Mechanism of S-type Phycobiliprotein Lyase CHAPERONE-LIKE ACTION AND FUNCTIONAL AMINO ACID RESIDUES