Characterization of an Aldolase−Dehydrogenase Complex That Exhibits Substrate Channeling in the Polychlorinated Biphenyls Degradation Pathway

Biochemistry ◽  
2009 ◽  
Vol 48 (27) ◽  
pp. 6551-6558 ◽  
Author(s):  
Perrin Baker ◽  
Dan Pan ◽  
Jason Carere ◽  
Adam Rossi ◽  
Weijun Wang ◽  
...  
Keyword(s):  
Polychlorinated Biphenyls ◽  
Degradation Pathway ◽  
Substrate Channeling ◽  
Dehydrogenase Complex

Characterization of an Aldolase–Dehydrogenase Complex from the Cholesterol Degradation Pathway ofMycobacterium tuberculosis

Biochemistry ◽  
2013 ◽  
Vol 52 (20) ◽  
pp. 3502-3511 ◽  
Author(s):  
Jason Carere ◽  
Sarah E. McKenna ◽  
Matthew S. Kimber ◽  
Stephen Y. K. Seah
Keyword(s):  
Degradation Pathway ◽  
Ofmycobacterium Tuberculosis ◽  
Dehydrogenase Complex

scholarly journals Protein complex formation in methionine chain-elongation and leucine biosynthesis

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Li-Qun Chen ◽  
Shweta Chhajed ◽  
Tong Zhang ◽  
Joseph M. Collins ◽  
Qiuying Pang ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Complete Characterization ◽  
Bimolecular Fluorescence Complementation ◽  
Chain Elongation ◽  
Substrate Channeling ◽  
Leucine Biosynthesis ◽  
Protein Complex Formation ◽  
Genes Encoding ◽  
Isopropylmalate Dehydrogenase

AbstractDuring the past two decades, glucosinolate (GLS) metabolic pathways have been under extensive studies because of the importance of the specialized metabolites in plant defense against herbivores and pathogens. The studies have led to a nearly complete characterization of biosynthetic genes in the reference plant Arabidopsis thaliana. Before methionine incorporation into the core structure of aliphatic GLS, it undergoes chain-elongation through an iterative three-step process recruited from leucine biosynthesis. Although enzymes catalyzing each step of the reaction have been characterized, the regulatory mode is largely unknown. In this study, using three independent approaches, yeast two-hybrid (Y2H), coimmunoprecipitation (Co-IP) and bimolecular fluorescence complementation (BiFC), we uncovered the presence of protein complexes consisting of isopropylmalate isomerase (IPMI) and isopropylmalate dehydrogenase (IPMDH). In addition, simultaneous decreases in both IPMI and IPMDH activities in a leuc:ipmdh1 double mutants resulted in aggregated changes of GLS profiles compared to either leuc or ipmdh1 single mutants. Although the biological importance of the formation of IPMI and IPMDH protein complexes has not been documented in any organisms, these complexes may represent a new regulatory mechanism of substrate channeling in GLS and/or leucine biosynthesis. Since genes encoding the two enzymes are widely distributed in eukaryotic and prokaryotic genomes, such complexes may have universal significance in the regulation of leucine biosynthesis.

scholarly journals Identification and Characterization of a Bacteroid-Specific Dehydrogenase Complex in Rhizobium leguminosarum PRE

1988 ◽  
Vol 54 (12) ◽  
pp. 3008-3013 ◽  
Author(s):  
René M. Klein Lankhorst ◽  
Panagiotis Katinakis ◽  
Albert van Kammen ◽  
Rommert C. van den Bos
Keyword(s):  
Rhizobium Leguminosarum ◽  
Identification And Characterization ◽  
Dehydrogenase Complex
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