PMID- 8830041
OWN - NLM
STAT- MEDLINE
DCOM- 19961017
LR  - 20191210
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 119
IP  - 3
DP  - 1996 Mar
TI  - Prolyl aminopeptidase is also present in Enterobacteriaceae: cloning and 
      sequencing of the Hafnia alvei enzyme-gene and characterization of the expressed 
      enzyme.
PG  - 468-74
AB  - The Hafnia alvei prolyl aminopeptidase gene (hpap) was cloned and sequenced, the 
      expressed enzyme (HPAP) was purified to homogeneity and thoroughly characterized. 
      An open reading frame of 1,281 bp was found to code for the enzyme, resulting in 
      a protein of 427 amino acids with a molecular weight of 48,577. HPAP resembles 
      the Aeromonas sobria enzyme, having 45% identity and the same distinctive 
      properties with respect to size and substrate specificities. Both enzyme show 
      similar chromatographic behavior, and HPAP could be purified following the 
      procedure previously described for the Aeromonas enzyme. HPAP was found to be 
      resistant to diisopropylphosphofluoridate as are most of the prolyl 
      aminopeptidases hitherto described. In spite of this similarity, no inhibition by 
      1 mM p-chloromercuribenzoate solution could be detected. Significant inhibition 
      was, however, observed when the enzyme was incubated with 
      3,4-dichloroisocoumarin. This study confirms the presence of two types of prolyl 
      aminopeptidases, of which the Hafnia and Aeromonas enzymes constitute one group 
      and the Bacillus, Neisseria, and Lactobacillus enzymes the other, and describes 
      the cloning of the first prolyl aminopeptidase gene from an Enterobacteriaceae.
FAU - Kitazono, A
AU  - Kitazono A
AD  - School of Pharmaceutical Sciences, Nagasaki University.
FAU - Kitano, A
AU  - Kitano A
FAU - Kabashima, T
AU  - Kabashima T
FAU - Ito, K
AU  - Ito K
FAU - Yoshimoto, T
AU  - Yoshimoto T
LA  - eng
SI  - GENBANK/D61383
PT  - Comparative Study
PT  - Journal Article
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Chloromercuribenzoates)
RN  - 0 (Coumarins)
RN  - 0 (DNA, Bacterial)
RN  - 0 (Isocoumarins)
RN  - 51050-59-0 (3,4-dichloroisocoumarin)
RN  - 59-85-8 (p-Chloromercuribenzoic Acid)
RN  - EC 3.4.11.- (Aminopeptidases)
RN  - EC 3.4.11.5 (prolyl aminopeptidase)
SB  - IM
MH  - Aeromonas/enzymology
MH  - Amino Acid Sequence
MH  - Aminopeptidases/*genetics/metabolism
MH  - Bacillus/enzymology
MH  - Base Sequence
MH  - Chloromercuribenzoates/pharmacology
MH  - Cloning, Molecular
MH  - Coumarins/pharmacology
MH  - DNA, Bacterial
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Enterobacteriaceae/*enzymology
MH  - Gene Expression Regulation, Enzymologic/*genetics
MH  - Isocoumarins
MH  - Lactobacillus/enzymology
MH  - Molecular Sequence Data
MH  - Neisseria/enzymology
MH  - Open Reading Frames/genetics
MH  - Restriction Mapping
MH  - Substrate Specificity
MH  - p-Chloromercuribenzoic Acid
EDAT- 1996/03/01 00:00
MHDA- 1996/03/01 00:01
CRDT- 1996/03/01 00:00
PHST- 1996/03/01 00:00 [pubmed]
PHST- 1996/03/01 00:01 [medline]
PHST- 1996/03/01 00:00 [entrez]
AID - 10.1093/oxfordjournals.jbchem.a021265 [doi]
PST - ppublish
SO  - J Biochem. 1996 Mar;119(3):468-74. doi: 10.1093/oxfordjournals.jbchem.a021265.