PMID- 10395453
OWN - NLM
STAT- MEDLINE
DCOM- 19990927
LR  - 20190921
IS  - 0277-8033 (Print)
IS  - 0277-8033 (Linking)
VI  - 18
IP  - 3
DP  - 1999 Apr
TI  - Structural investigations on human erythrocyte acylpeptide hydrolase by mass
      spectrometric procedures.
PG  - 349-60
AB  - The complete primary structure of human erythrocyte acylpeptide hydrolase has
      been determined by using a combination of different mass spectrometric procedures
      and sequencing techniques. These data allowed us to correct the incomplete
      nucleotide sequence of the DNF15S2 locus on the short arm of human chromosome 3
      at region 21, coding for the enzyme. The protein consists of 732 amino acid
      residues and is acetylated at the N-terminus. Alkylation experiments on the
      native enzyme demonstrated that all 17 cysteine residues present in the
      polypeptide chain are in reduced form. Multiple sequence alignment did not reveal
      striking similarity with proteases of known tertiary structure with the exception
      of members of the serine oligopeptidase family. Limited proteolysis experiments
      generated a C-terminal portion, containing all the catalytic triad elements
      responsible for proteolytic activity, and an N-terminal domain of unknown
      function, both still strongly associated in a completely active nicked form. The 
      site of tryptic hydrolysis was identified as Arg193. The secondary structural
      organization of the protease domain of the enzyme is consistent with the
      alpha/beta hydrolase fold.
FAU - Scaloni, A
AU  - Scaloni A
AD  - Centro Internazionale Servizi di Spettrometria di Massa, C.N.R-Universita' di
      Napoli Federico II, Naples, Italy. ascaloni@saul.iabbam.na.cnr.it
FAU - Ingallinella, P
AU  - Ingallinella P
FAU - Andolfo, A
AU  - Andolfo A
FAU - Jones, W
AU  - Jones W
FAU - Marino, G
AU  - Marino G
FAU - Manning, J M
AU  - Manning JM
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Protein Chem
JT  - Journal of protein chemistry
JID - 8217321
RN  - EC 3.4.- (Peptide Hydrolases)
RN  - EC 3.4.19.1 (acylaminoacyl-peptidase)
RN  - EC 3.4.21.4 (Trypsin)
RN  - K848JZ4886 (Cysteine)
SB  - IM
MH  - Alkylation
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cysteine/metabolism
MH  - Erythrocytes/*enzymology
MH  - Humans
MH  - Mass Spectrometry/*methods
MH  - Molecular Sequence Data
MH  - Oxidation-Reduction
MH  - Peptide Hydrolases/*analysis
MH  - Protein Processing, Post-Translational
MH  - Rats
MH  - Sequence Homology, Amino Acid
MH  - Swine
MH  - Time Factors
MH  - Trypsin/metabolism
EDAT- 1999/07/08 00:00
MHDA- 1999/07/08 00:01
CRDT- 1999/07/08 00:00
PHST- 1999/07/08 00:00 [pubmed]
PHST- 1999/07/08 00:01 [medline]
PHST- 1999/07/08 00:00 [entrez]
AID - 10.1023/a:1021047730831 [doi]
PST - ppublish
SO  - J Protein Chem. 1999 Apr;18(3):349-60. doi: 10.1023/a:1021047730831.