Characterization of a Plasmodium vivax Cysteine Proteinase Gene Identifies Uniquely Conserved Amino Acids that May Mediate the Substrate Specificity of Malarial Hemoglobinases

1994 ◽  
Vol 241 (2) ◽  
pp. 312-316 ◽  
Author(s):  
Philip J. Rosenthal ◽  
Christine S. Ring ◽  
Xiaowu Chen ◽  
Fred E. Cohen
Keyword(s):  
Amino Acids ◽  
Substrate Specificity ◽  
Plasmodium Vivax ◽  
Cysteine Proteinase ◽  
Conserved Amino Acids

scholarly journals Molecular cloning and characterization of ornithine decarboxylase cDNA of the nematode Panagrellus redivivus

1995 ◽  
Vol 308 (2) ◽  
pp. 635-640 ◽  
Author(s):  
H von Besser ◽  
G Niemann ◽  
B Domdey ◽  
R D Walter
Keyword(s):  
Amino Acids ◽  
Active Sites ◽  
Cdna Clones ◽  
Degenerate Primers ◽  
Calculated Molecular Mass ◽  
Panagrellus Redivivus ◽  
Free Living Nematode ◽  
Mixed Stage ◽  
Conserved Amino Acids

In a PCR with degenerate primers encoding highly conserved amino acids within ornithine decarboxylases (ODCs) of several organisms, a fragment of the ODC gene of the free-living nematode Panagrellus redivivus was isolated. Northern blot analysis revealed a single 1.7 kb transcript in a mixed-stage population of animals. From this RNA source, a cDNA library was constructed and screened with the PCR fragment. Several cDNA clones were isolated, one of which encodes the complete 435-amino-acid ODC enzyme with a calculated molecular mass of 47.1 kDa. The P. redivivus ODC possesses 126 of the 136 highly conserved amino acids in the enzymes from fungi, invertebrates and vertebrates. Functional amino acids are conserved, suggesting that the two active sites of the P. redivivus ODC are formed at the interface of a homodimer, as described for mammalian ODCs.

scholarly journals Characterization of the Amino Acids fromNeisseria meningitidisMethionine Sulfoxide Reductase B Involved in the Chemical Catalysis and Substrate Specificity of the Reductase Step

2007 ◽  
Vol 282 (44) ◽  
pp. 32397-32405 ◽  
Author(s):  
Fabrice Neiers ◽  
Sanjiv Sonkaria ◽  
Alexandre Olry ◽  
Sandrine Boschi-Muller ◽  
Guy Branlant
Keyword(s):  
Amino Acids ◽  
Substrate Specificity ◽  
Chemical Catalysis

scholarly journals Functional and structural characterization of IdnL7, an adenylation enzyme involved in incednine biosynthesis

2019 ◽  
Vol 75 (4) ◽  
pp. 299-306
Author(s):  
Jolanta Cieślak ◽  
Akimasa Miyanaga ◽  
Makoto Takaishi ◽  
Fumitaka Kudo ◽  
Tadashi Eguchi
Keyword(s):  
Amino Acids ◽  
Substrate Specificity ◽  
Natural Product ◽  
Structural Characterization ◽  
Biochemical Analysis ◽  
Natural Product Biosynthesis ◽  
Broad Substrate Specificity ◽  
Selective Incorporation ◽  
Polyketide Antibiotic

Adenylation enzymes play an important role in the selective incorporation of the cognate carboxylate substrates in natural product biosynthesis. Here, the biochemical and structural characterization of the adenylation enzyme IdnL7, which is involved in the biosynthesis of the macrolactam polyketide antibiotic incednine, is reported. Biochemical analysis showed that IdnL7 selects and activates several small amino acids. The structure of IdnL7 in complex with an L-alanyl-adenylate intermediate mimic, 5′-O-[N-(L-alanyl)sulfamoyl]adenosine, was determined at 2.1 Å resolution. The structure of IdnL7 explains the broad substrate specificity of IdnL7 towards small L-amino acids.

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