PMID- 23499933
OWN - NLM
STAT- MEDLINE
DCOM- 20131231
LR  - 20130508
IS  - 1879-0240 (Electronic)
IS  - 0965-1748 (Linking)
VI  - 43
IP  - 6
DP  - 2013 Jun
TI  - A digestive prolyl carboxypeptidase in Tenebrio molitor larvae.
PG  - 501-9
LID - S0965-1748(13)00033-7 [pii]
LID - 10.1016/j.ibmb.2013.02.009 [doi]
AB  - Prolyl carboxypeptidase (PRCP) is a lysosomal proline specific serine peptidase 
      that also plays a vital role in the regulation of physiological processes in 
      mammals. In this report, we isolate and characterize the first PRCP in an insect. 
      PRCP was purified from the anterior midgut of larvae of a stored product pest, 
      Tenebrio molitor, using a three-step chromatography strategy, and it was 
      determined that the purified enzyme was a dimer. The cDNA of PRCP was cloned and 
      sequenced, and the predicted protein was identical to the proteomic sequences of 
      the purified enzyme. The substrate specificity and kinetic parameters of the 
      enzyme were determined. The T. molitor PRCP participates in the hydrolysis of the 
      insect's major dietary proteins, gliadins, and is the first PRCP to be ascribed a 
      digestive function. Our collective data suggest that the evolutionary enrichment 
      of the digestive peptidase complex in insects with an area of acidic to neutral 
      pH in the midgut is a result of the incorporation of lysosomal peptidases, 
      including PRCP.
CI  - Published by Elsevier Ltd.
FAU - Goptar, Irina A
AU  - Goptar IA
AD  - Chemical Faculty, Moscow State University, Moscow 119991, Russia.
FAU - Shagin, Dmitry A
AU  - Shagin DA
FAU - Shagina, Irina A
AU  - Shagina IA
FAU - Mudrik, Elena S
AU  - Mudrik ES
FAU - Smirnova, Yulia A
AU  - Smirnova YA
FAU - Zhuzhikov, Dmitry P
AU  - Zhuzhikov DP
FAU - Belozersky, Mikhail A
AU  - Belozersky MA
FAU - Dunaevsky, Yakov E
AU  - Dunaevsky YE
FAU - Oppert, Brenda
AU  - Oppert B
FAU - Filippova, Irina Yu
AU  - Filippova IY
FAU - Elpidina, Elena N
AU  - Elpidina EN
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130314
PL  - England
TA  - Insect Biochem Mol Biol
JT  - Insect biochemistry and molecular biology
JID - 9207282
RN  - EC 1.14.11.- (Prolyl Hydroxylases)
RN  - EC 3.4.- (Carboxypeptidases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Carboxypeptidases/chemistry/genetics/*isolation & purification
MH  - Digestive System/*enzymology
MH  - Hydrolysis
MH  - Larva/enzymology/genetics
MH  - Molecular Sequence Data
MH  - Prolyl Hydroxylases/*chemistry/genetics/isolation & purification
MH  - Substrate Specificity
MH  - Tenebrio/*enzymology/genetics
EDAT- 2013/03/19 06:00
MHDA- 2014/01/01 06:00
CRDT- 2013/03/19 06:00
PHST- 2012/11/13 00:00 [received]
PHST- 2013/02/27 00:00 [revised]
PHST- 2013/02/28 00:00 [accepted]
PHST- 2013/03/19 06:00 [entrez]
PHST- 2013/03/19 06:00 [pubmed]
PHST- 2014/01/01 06:00 [medline]
AID - S0965-1748(13)00033-7 [pii]
AID - 10.1016/j.ibmb.2013.02.009 [doi]
PST - ppublish
SO  - Insect Biochem Mol Biol. 2013 Jun;43(6):501-9. doi: 10.1016/j.ibmb.2013.02.009. 
      Epub 2013 Mar 14.