Chitotriosidase, a prematurely orphan enzyme

2004 ◽  
Vol 19 (1) ◽  
pp. 71-75 ◽  
Author(s):  
L. Malaguarnera ◽  
R. Barone ◽  
A. Angius ◽  
S. Musumeci
Keyword(s):  
Orphan Enzyme

scholarly journals ORENZA: a web resource for studying ORphan ENZyme activities

2006 ◽  
Vol 7 (1) ◽  
Author(s):  
Olivier Lespinet ◽  
Bernard Labedan
Keyword(s):  
Enzyme Activities ◽  
Web Resource ◽  
Orphan Enzyme ◽  
Orphan Enzyme Activities

scholarly journals Arabidopsis TH2 Encodes the Orphan Enzyme Thiamin Monophosphate Phosphatase

2016 ◽  
Vol 28 (10) ◽  
pp. 2683-2696 ◽  
Author(s):  
Manaki Mimura ◽  
Rémi Zallot ◽  
Thomas D. Niehaus ◽  
Ghulam Hasnain ◽  
Satinder K. Gidda ◽  
...  
Keyword(s):  
Orphan Enzyme

scholarly journals Discovery of a novel stereospecific β-hydroxyacyl-CoA lyase/thioesterase shared by three metabolic pathways in Mycobacterium tuberculosis

2018 ◽  
Author(s):  
Hua Wang ◽  
Alexander A. Fedorov ◽  
Elena V. Fedorov ◽  
Deborah M. Hunt ◽  
Angela Rodgers ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Metabolic Pathways ◽  
Resistance Mechanism ◽  
Physiological Role ◽  
Vast Number ◽  
X Ray Crystallography ◽  
Leucine Catabolism ◽  
Orphan Enzyme

AbstractThe vast number of poorly characterised enzymes in Mycobacterium tuberculosis (Mtb) is one of the key barriers precluding a better understanding of the biology that underpins pathogenesis. Here, we investigated the Mtb orphan enzyme Rv2498c to delineate its physiological role. Our results from in vitro enzymatic assays, phylogenetic analysis, X-ray crystallography and in vivo Mtb experiments, de-orphan Rv2498c as a multi-functional β-hydroxyacyl-CoA lyase/thioesterase (β-HAClyase/thioesterase) that participates in three different metabolic pathways: L-leucine catabolism, itaconate dissimilation, and glyoxylate shunt. Moreover, the deletion of the rv2498c gene from the Mtb genome resulted in attenuation in the mouse model compared to infection with the parent strain. To the best of our knowledge, this is the first report of an (R)-3-hydroxyl-3-methylglutaryl-CoA for leucine catabolism and an itaconate-specific resistance mechanism in Mtb.

Caspase-2: an orphan enzyme out of the shadows

Oncogene ◽  
2017 ◽  
Vol 36 (39) ◽  
pp. 5441-5444 ◽  
Author(s):  
J Forsberg ◽  
B Zhivotovsky ◽  
M Olsson
Keyword(s):  
Caspase 2 ◽  
Orphan Enzyme

scholarly journals Rescue of the Orphan Enzyme Isoguanine Deaminase

Biochemistry ◽  
2011 ◽  
Vol 50 (25) ◽  
pp. 5555-5557 ◽  
Author(s):  
Daniel S. Hitchcock ◽  
Alexander A. Fedorov ◽  
Elena V. Fedorov ◽  
Lawrence J. Dangott ◽  
Steven C. Almo ◽  
...  
Keyword(s):  
Orphan Enzyme

scholarly journals Orphan enzyme cuts down on sugar

2014 ◽  
Vol 33 (24) ◽  
pp. 2883-2884
Author(s):  
Siniša Urban
Keyword(s):  
Orphan Enzyme

scholarly journals A survey of orphan enzyme activities

2007 ◽  
Vol 8 (1) ◽  
Author(s):  
Yannick Pouliot ◽  
Peter D Karp
Keyword(s):  
Enzyme Activities ◽  
Orphan Enzyme ◽  
Orphan Enzyme Activities

scholarly journals Orphan enzyme or patriarch of a new tribe: the arsenic resistance ATPase of bacterial plasmids

1993 ◽  
Vol 8 (4) ◽  
pp. 637-642 ◽  
Author(s):  
Simon Silver ◽  
Guangyong Ji ◽  
Stefan Bröer ◽  
Saibal Dey ◽  
Dexian Dou ◽  
...  
Keyword(s):  
Arsenic Resistance ◽  
Bacterial Plasmids ◽  
New Tribe ◽  
Orphan Enzyme

Crystal structures and functional studies clarify substrate selectivity and catalytic residues for the unique orphan enzyme N-acetyl-D-mannosamine dehydrogenase

2014 ◽  
Vol 462 (3) ◽  
pp. 499-511 ◽  
Author(s):  
Agustín Sola-Carvajal ◽  
Fernando Gil-Ortiz ◽  
Francisco García-Carmona ◽  
Vicente Rubio ◽  
Álvaro Sánchez-Ferrer
Keyword(s):  
Substrate Specificity ◽  
Crystal Structures ◽  
Functional Site ◽  
Site Directed Mutagenesis ◽  
Short Chain ◽  
Directed Mutagenesis ◽  
Substrate Selectivity ◽  
Functional Studies ◽  
Short Chain Dehydrogenase ◽  
Orphan Enzyme

Functional site-directed mutagenesis and crystallographic studies with N-acetyl-D-mannosamine dehydrogenase reveal a homotetramer, a short-chain dehydrogenase/reductase subunit fold and a highly developed C-terminal tail interlinking subunit. The structures of the complexes explain substrate specificity. The four residues forming the catalytic tetrad are identified.

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