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A mutant of phosphomannomutase1 retains full enzymatic activity, but is not activated by IMP: Possible implications for the disease PMM2-CDG.

Abstract The most frequent disorder of glycosylation, PMM2-CDG, is caused by a deficiency of phosphomannomutase activity. In humans two paralogous enzymes exist, both of them require mannose 1,6-bis-phosphate or glucose 1,6-bis-phosphate as activators, but only phospho-mannomutase1 hydrolyzes bis-phosphate hexoses. Mutations in the gene encoding phosphomannomutase2 are responsible for PMM2-CDG. Although not directly causative of the disease, the role of the paralogous enzyme in the disease should be clarified. Phosphomannomutase1 could have a beneficial effect, contributing to mannose 6-phosphate isomerization, or a detrimental effect, hydrolyzing the bis-phosphate hexose activator. A pivotal role in regulating mannose-1phosphate production and ultimately protein glycosylation might be played by inosine monophosphate that enhances the phosphatase activity of phosphomannomutase1. In this paper we analyzed human phosphomannomutases by conventional enzymatic assays as well as by novel techniques such as 31P-NMR and thermal shift assay. We characterized a triple mutant of phospomannomutase1 that retains mutase and phosphatase activity, but is unable to bind inosine monophosphate.
PMID
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Authors

Mayor MeshTerms
Keywords
Journal Title plos one
Publication Year Start




PMID- 29261720
OWN - NLM
STAT- MEDLINE
DCOM- 20180108
LR  - 20180108
IS  - 1932-6203 (Electronic)
IS  - 1932-6203 (Linking)
VI  - 12
IP  - 12
DP  - 2017
TI  - A mutant of phosphomannomutase1 retains full enzymatic activity, but is not
      activated by IMP: Possible implications for the disease PMM2-CDG.
PG  - e0189629
LID - 10.1371/journal.pone.0189629 [doi]
AB  - The most frequent disorder of glycosylation, PMM2-CDG, is caused by a deficiency 
      of phosphomannomutase activity. In humans two paralogous enzymes exist, both of
      them require mannose 1,6-bis-phosphate or glucose 1,6-bis-phosphate as
      activators, but only phospho-mannomutase1 hydrolyzes bis-phosphate hexoses.
      Mutations in the gene encoding phosphomannomutase2 are responsible for PMM2-CDG. 
      Although not directly causative of the disease, the role of the paralogous enzyme
      in the disease should be clarified. Phosphomannomutase1 could have a beneficial
      effect, contributing to mannose 6-phosphate isomerization, or a detrimental
      effect, hydrolyzing the bis-phosphate hexose activator. A pivotal role in
      regulating mannose-1phosphate production and ultimately protein glycosylation
      might be played by inosine monophosphate that enhances the phosphatase activity
      of phosphomannomutase1. In this paper we analyzed human phosphomannomutases by
      conventional enzymatic assays as well as by novel techniques such as 31P-NMR and 
      thermal shift assay. We characterized a triple mutant of phospomannomutase1 that 
      retains mutase and phosphatase activity, but is unable to bind inosine
      monophosphate.
FAU - Citro, Valentina
AU  - Citro V
AD  - Dipartimento di Biologia, Universita Federico II, Napoli, Italy.
FAU - Cimmaruta, Chiara
AU  - Cimmaruta C
AD  - Dipartimento di Biologia, Universita Federico II, Napoli, Italy.
FAU - Liguori, Ludovica
AU  - Liguori L
AD  - Istituto di Chimica Biomolecolare-CNR, Pozzuoli, Italy.
AD  - Dipartimento di scienze e tecnologie ambientali, biologiche e farmaceutiche,
      Universita della Campania "Luigi Vanvitelli", Caserta, Italy.
FAU - Viscido, Gaetano
AU  - Viscido G
AD  - Dipartimento di Biologia, Universita Federico II, Napoli, Italy.
FAU - Cubellis, Maria Vittoria
AU  - Cubellis MV
AUID- ORCID: http://orcid.org/0000-0001-6147-6553
AD  - Dipartimento di Biologia, Universita Federico II, Napoli, Italy.
AD  - Istituto di Chimica Biomolecolare-CNR, Pozzuoli, Italy.
FAU - Andreotti, Giuseppina
AU  - Andreotti G
AD  - Istituto di Chimica Biomolecolare-CNR, Pozzuoli, Italy.
LA  - eng
PT  - Journal Article
DEP - 20171219
PL  - United States
TA  - PLoS One
JT  - PloS one
JID - 101285081
RN  - 0 (Diphosphonates)
RN  - 0 (Ligands)
RN  - 131-99-7 (Inosine Monophosphate)
RN  - EC 5.4.2.- (Phosphotransferases (Phosphomutases))
RN  - EC 5.4.2.8 (phosphomannomutase)
RN  - Congenital disorder of glycosylation type 1A
SB  - IM
MH  - Amino Acid Sequence
MH  - Congenital Disorders of Glycosylation/*enzymology/*genetics
MH  - Diphosphonates/pharmacology
MH  - Enzyme Activation/drug effects
MH  - Enzyme Assays
MH  - Enzyme Stability/drug effects
MH  - Humans
MH  - Inosine Monophosphate/*pharmacology
MH  - Ligands
MH  - Magnetic Resonance Spectroscopy
MH  - Molecular Docking Simulation
MH  - Mutation/*genetics
MH  - Phosphotransferases (Phosphomutases)/chemistry/*deficiency/genetics
MH  - Sequence Alignment
MH  - Temperature
PMC - PMC5736207
EDAT- 2017/12/21 06:00
MHDA- 2018/01/09 06:00
CRDT- 2017/12/21 06:00
PHST- 2017/07/26 00:00 [received]
PHST- 2017/11/29 00:00 [accepted]
PHST- 2017/12/21 06:00 [entrez]
PHST- 2017/12/21 06:00 [pubmed]
PHST- 2018/01/09 06:00 [medline]
AID - 10.1371/journal.pone.0189629 [doi]
AID - PONE-D-17-27965 [pii]
PST - epublish
SO  - PLoS One. 2017 Dec 19;12(12):e0189629. doi: 10.1371/journal.pone.0189629.
      eCollection 2017.