Document Detail

Cloning, expression, and characterization of a methionyl aminopeptidase from a hyperthermophilic archaeon Thermococcus sp. NA1.
MedLine Citation:
PMID:  16761197     Owner:  NLM     Status:  MEDLINE    
Genomic analysis of a hyperthermophilic archaeon Thermococcus sp. NA1 revealed the presence of an 885-bp open reading frame encoding a protein of 295 amino acids with a calculated molecular mass of 32,981 Da. Analysis of the deduced amino acid sequence showed that amino acid residues important for catalytic activity and the metal binding ligands conserved in all of methionyl aminopeptidases (MetAP) were also conserved and belonged to type IIa MetAP. The protein, designated TNA1_MetAP (Thermococcus sp. NA1 MetAP), was cloned and expressed in Escherichia coli. The recombinant enzyme was a Mn(2+)-, Ni(2+)-, Fe(2+)-, or Co(2+)-dependent metallopeptidase. Optimal MetAP activity against L: -methionine p-nitroanilide (Met-pNA) (K (m) = 0.68 mM) occurred at pH 7.0 and 80 to 90 degrees C. The MetAP was very unstable compared to Pyrococcus furiosus MetAP, which was completely inactivated by heating at 80 degrees C for 5 min. It seemed likely that the cysteine residue (Cys53) played a critical role in regulating the thermostability of TNA1_MetAP.
H S Lee; Y J Kim; S S Bae; J H Jeon; J K Lim; B C Jeong; S G Kang; J-H Lee
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-06-12
Journal Detail:
Title:  Marine biotechnology (New York, N.Y.)     Volume:  8     ISSN:  1436-2228     ISO Abbreviation:  Mar. Biotechnol.     Publication Date:    2006 Jul-Aug
Date Detail:
Created Date:  2006-08-10     Completed Date:  2007-10-25     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  100892712     Medline TA:  Mar Biotechnol (NY)     Country:  United States    
Other Details:
Languages:  eng     Pagination:  425-32     Citation Subset:  IM    
Korean Ocean Research & Development Institute, Ansan, P.O. Box 29, Seoul, 425-600, Korea.
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MeSH Terms
Amino Acid Sequence
Aminopeptidases / biosynthesis*,  chemistry,  drug effects,  genetics*
Cloning, Molecular / methods
DNA Primers / chemistry
Escherichia coli / genetics
Hot Temperature
Metals / pharmacology
Molecular Sequence Data
Oceans and Seas
Recombinant Proteins / biosynthesis,  drug effects,  genetics,  metabolism
Sequence Alignment
Thermococcus / enzymology*,  genetics*,  physiology
Time Factors
Reg. No./Substance:
0/DNA Primers; 0/Metals; 0/Recombinant Proteins; EC 3.4.11.-/Aminopeptidases; EC aminopeptidase

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