scholarly journals Biochemical Properties and Potential Applications of Recombinant Leucine Aminopeptidase from Bacillus kaustophilus CCRC 11223

2011 ◽  
Vol 12 (11) ◽  
pp. 7609-7625 ◽  
Author(s):  
Yanfei Shen ◽  
Fanghua Wang ◽  
Dongming Lan ◽  
Yuanyuan Liu ◽  
Bo Yang ◽  
...  
Keyword(s):  
Leucine Aminopeptidase ◽  
Biochemical Properties ◽  
Bacillus Kaustophilus ◽  
Potential Applications

Synthesis and biochemical properties of the novel, enzymatically stable mRNA cap analogues with versatile potential applications

2005 ◽  
Author(s):  
Marcin Kalek ◽  
Jacek Jemielity ◽  
Ewa Grudzien ◽  
Joanna Zuberek ◽  
Zbigniew M. Darzynkiewicz ◽  
...  
Keyword(s):  
Biochemical Properties ◽  
The Novel ◽  
Potential Applications

Characterization of Bacillus kaustophilus leucine aminopeptidase immobilized in Ca-alginate/k-carrageenan beads

2008 ◽  
Vol 39 (2) ◽  
pp. 376-382 ◽  
Author(s):  
Meng-Chun Chi ◽  
Rui-Cin Lyu ◽  
Long-Liu Lin ◽  
Hsien-Bin Huang
Keyword(s):  
Leucine Aminopeptidase ◽  
Bacillus Kaustophilus ◽  
Ca Alginate

scholarly journals Biochemical characteristics of Streptococcus suis strains isolated from healthy and deceased pigs

2014 ◽  
Vol 30 (4) ◽  
pp. 699-704 ◽  
Author(s):  
А. Stanojkovic ◽  
М.M. Petrovic ◽  
Z. Skrbic ◽  
V. Mandic ◽  
N. Stanisic ◽  
...  
Keyword(s):  
Bacterial Infection ◽  
Leucine Aminopeptidase ◽  
Clinical Signs ◽  
Streptococcus Suis ◽  
Biochemical Properties ◽  
Biochemical Tests ◽  
Biochemical Characteristics ◽  
Arginine Dihydrolase ◽  
Specific Antisera ◽  
Phenyl Alanine

The aim of this study was to determine the biochemical properties of Streptococcus suis strains isolated from healthy and deceased pigs. For this research we tested 34 S. suis strains isolated from deceased pigs that had clinical signs of septicemia and meningitis, as well as from clinically healthy pigs. The strains that have been already confirmed with specific antisera were tested using commercial battery of biochemical tests (API 20 Strep and ID 32 Strep) to determine the dominant biochemical characteristics that can be used in diagnosis of bacterial infection if specific S. suis antisera are not available. The main results showed that all S. suis strains were postive in esculine, trehalose, glycogen, lactose, sacharose, starch, leucine aminopeptidase, alanine-phenyl-alanine-proline arylamidase tests, while negative in Voges-Proskauer, hipurate, ribose, arabinose and sorbitol tests. S. suis strains were in high percentage positive in arginine dihydrolase, ?-glucoronidase, ?-galactosidase, ?-galactosidase, methyl-?-dglucopyranoside, glycyl-tryptophan arylamidase and inulin tests. Athough S. suis is in highly positive in some tests, it can be concluded that Voges-Proskauer, hipurate, trehalose, esculine tests, along with ?-glucoronidase (?GUR) and ?- galactosidase (?GAL), were significant in differentiation of this bacteria from other similar streptococci, along with some other crucial features (? hemolysis on blood sheep agar, absence of growth in 6,5% NaCl broth).

Molecular cloning and characterization of a M17 leucine aminopeptidase of Cryptosporidium parvum

Parasitology ◽  
2011 ◽  
Vol 138 (6) ◽  
pp. 682-690 ◽  
Author(s):  
J.-M. KANG ◽  
H.-L. JU ◽  
W.-M. SOHN ◽  
B.-K. NA
Keyword(s):  
Amino Acid ◽  
Cryptosporidium Parvum ◽  
Metal Binding ◽  
Drug Targets ◽  
Leucine Aminopeptidase ◽  
Biochemical Properties ◽  
Site Formation ◽  
Amino Acid Residues ◽  
Multiple Sequence ◽  
Binding Characteristics

SUMMARYLeucine aminopeptidases (LAPs) are a group of metalloexopeptidases that catalyse the sequential removal of amino acids from the N-termini of polypeptides or proteins. They play an important role in regulating the balance between catabolism and anabolism in living cells. LAPs of apicomplexa parasitic protozoa have been intensively investigated due to their crucial roles in parasite biology as well as their potentials as drug targets. In this study, we identified an M17 leucine aminopeptidase of Cryptosporidium parvum (CpLAP) and characterized the biochemical properties of the recombinant protein. Multiple sequence alignment of the deduced amino acid sequence of CpLAP with those of other organisms revealed that typical amino acid residues essential for metal binding and active-site formation in M17 LAPs were well conserved in CpLAP. Recombinant CpLAP shared similar biochemical properties such as optimal pH, stability at neutral pHs, and metal-binding characteristics with other characterized LAPs. The enzyme showed a marked preference for Leu and its activity was effectively inhibited by bestatin. These results collectively suggest that CpLAP is a typical member of the M17 LAP family and may play an important role in free amino acid regulation in the parasite.

scholarly journals Biochemical and structural exploration of the catalytic capacity of Sulfolobus KDG aldolases

2007 ◽  
Vol 403 (3) ◽  
pp. 421-430 ◽  
Author(s):  
Suzanne Wolterink-van Loo ◽  
André van Eerde ◽  
Marco A. J. Siemerink ◽  
Jasper Akerboom ◽  
Bauke W. Dijkstra ◽  
...  
Keyword(s):  
Biochemical Properties ◽  
Binding Motif ◽  
Phosphate Binding ◽  
Sulfolobus Tokodaii ◽  
Acceptor Substrate ◽  
Hydrogen Bonding Interactions ◽  
Potential Applications ◽  
Multiple Hydrogen Bonding ◽  
Multiple Conformations ◽  
Catalytic Capacity

Aldolases are enzymes with potential applications in biosynthesis, depending on their activity, specificity and stability. In the present study, the genomes of Sulfolobus species were screened for aldolases. Two new KDGA [2-keto-3-deoxygluconate (2-oxo-3-deoxygluconate) aldolases] from Sulfolobus acidocaldarius and Sulfolobus tokodaii were identified, overexpressed in Escherichia coli and characterized. Both enzymes were found to have biochemical properties similar to the previously characterized S. solfataricus KDGA, including the condensation of pyruvate and either D,L-glyceraldehyde or D,L-glyceraldehyde 3-phosphate. The crystal structure of S. acidocaldarius KDGA revealed the presence of a novel phosphate-binding motif that allows the formation of multiple hydrogen-bonding interactions with the acceptor substrate, and enables high activity with glyceraldehyde 3-phosphate. Activity analyses with unnatural substrates revealed that these three KDGAs readily accept aldehydes with two to four carbon atoms, and that even aldoses with five carbon atoms are accepted to some extent. Water-mediated interactions permit binding of substrates in multiple conformations in the spacious hydrophilic binding site, and correlate with the observed broad substrate specificity.

scholarly journals Residues threonine 346 and leucine 352 are critical for the proper function of Bacillus kaustophilus leucine aminopeptidase

2006 ◽  
Vol 260 (2) ◽  
pp. 156-161 ◽  
Author(s):  
Meng-Chun Chi ◽  
Hsien-Ben Huang ◽  
Jai-Shin Liu ◽  
Wen-Ching Wang ◽  
Wan-Chi Liang ◽  
...  
Keyword(s):  
Leucine Aminopeptidase ◽  
Proper Function ◽  
Bacillus Kaustophilus
Sign in / Sign up

Export Citation Format

Share Document