EzCatDB: T00101
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DB codeT00101
RLCP classification8.131.584400.264 : Isomerization
8.113.904870.263 : Isomerization
CATH domainDomain 12.60.120.10 : Jelly RollsCatalytic domain
Domain 21.10.441.10 : Phosphomannose Isomerase; domain 2
Domain 32.60.120.10 : Jelly Rolls
E.C.5.3.1.8
CSA1pmi

CATH domainRelated DB codes (homologues)
2.60.120.10 : Jelly RollsS00145,S00155,D00842,D00843,T00255,M00216

Enzyme Name
UniProtKBKEGG

P34948
Protein nameMannose-6-phosphate isomerasemannose-6-phosphate isomerase
phosphomannose isomerase
phosphohexomutase
phosphohexoisomerase
mannose phosphate isomerase
phosphomannoisomerase
D-mannose-6-phosphate ketol-isomerase
SynonymsEC 5.3.1.8
Phosphohexomutase
Phosphomannose isomerase
PMI
RefSeqXP_714562.1 (Protein)
XM_709469.1 (DNA/RNA sequence)
PfamPF01238 (PMI_typeI)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00051Fructose and mannose metabolism

UniProtKB:Accession NumberP34948
Entry nameMPI_CANAL
ActivityD-mannose 6-phosphate = D-fructose 6- phosphate.
SubunitMonomer.
Subcellular locationCytoplasm (Probable).
CofactorBinds 1 zinc ion per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00038C00275C00085
CompoundZincD-Mannose 6-phosphateD-Fructose 6-phosphate
Typeheavy metalcarbohydrate,phosphate group/phosphate ioncarbohydrate,phosphate group/phosphate ion
ChEBI29105
48066
61553
PubChem32051
65127
439160
           
1pmiA01Bound:_ZNUnboundUnbound
1pmiA02UnboundUnboundUnbound
1pmiA03UnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P34948 & literature [6]
pdbCatalytic residuesCofactor-binding residues
          
1pmiA01LYS 136;TYR 287;GLU 294
GLN 111;HIS 113;GLU 138;HIS 285(Zinc binding)
1pmiA02 
 
1pmiA03 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]FIGURE 7, p.5781-5782
[6]p.477
[11]FIGURE 8, p.2932

references
[1]
PubMed ID1660728
JournalBiochimie
Year1991
Volume73
Pages1241-4
AuthorsWillem R, Malaisse-Lagae F, Malaisse WJ
TitlePhosphoglucoisomerase-catalyzed interconversion of hexose phosphates: distinction of the 1-monodeutero-isotopomers of D-fructose 6-phosphate by 1H NMR spectroscopy.
[2]
PubMed ID1448058
JournalMol Cell Biochem
Year1992
Volume115
Pages137-42
AuthorsMalaisse-Lagae F, Willem R, Penders M, Malaisse WJ
TitleDual anomeric specificity of phosphomannoisomerase assessed by 2D phase sensitive 13C EXSY NMR.
[3]
CommentsCHEMICAL LABELLING OF CYS-149, AND PARTIAL PROTEIN SEQUENCE.
PubMed ID8260497
JournalBiochemistry
Year1993
Volume32
Pages14139-44
AuthorsCoulin F, Magnenat E, Proudfoot AE, Payton MA, Scully P, Wells TN
TitleIdentification of Cys-150 in the active site of phosphomannose isomerase from Candida albicans.
[4]
CommentsACTIVE SITE ARG-303, AND SEQUENCE OF 299-311.
Medline ID94235645
PubMed ID8180205
JournalBiochemistry
Year1994
Volume33
Pages5777-82
AuthorsWells TN, Scully P, Magnenat E
TitleArginine 304 is an active site residue in phosphomannose isomerase from Candida albicans.
Related UniProtKBP34948
[5]
PubMed ID8145246
JournalJ Mol Biol
Year1994
Volume237
Pages349-50
AuthorsTolley S, Davies G, Hubbard RE, Smith DJ, Proudfoot AE, Payton MA, Cleasby A, Wonacott A, Wells TN
TitleCrystallization and preliminary X-ray analysis of Candida albicans phosphomannose isomerase.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
Medline ID96196885
PubMed ID8612079
JournalNat Struct Biol
Year1996
Volume3
Pages470-9
AuthorsCleasby A, Wonacott A, Skarzynski T, Hubbard RE, Davies GJ, Proudfoot AE, Bernard AR, Payton MA, Wells TN
TitleThe x-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution.
Related PDB1pmi
Related UniProtKBP34948
[7]
PubMed ID9118997
JournalEur J Biochem
Year1997
Volume244
Pages325-33
AuthorsSmith JJ, Thomson AJ, Proudfoot AE, Wells TN
TitleIdentification of an Fe(III)-dihydroxyphenylalanine site in recombinant phosphomannose isomerase from Candida albicans.
[8]
PubMed ID9507048
JournalBiochim Biophys Acta
Year1998
Volume1382
Pages5-7
AuthorsJensen SO, Reeves PR
TitleDomain organisation in phosphomannose isomerases (types I and II).
[9]
PubMed ID11697049
JournalJ Enzyme Inhib
Year2001
Volume16
Pages287-92
AuthorsSalvati L, Mattu M, Tiberi F, Polticelli F, Ascenzi P
TitleInhibition of Saccharomyces cerevisiae phosphomannose isomerase by the NO-donor S-nitroso-acetyl-penicillamine.
[10]
PubMed ID12042299
JournalJ Biol Chem
Year2002
Volume277
Pages26351-5
AuthorsHewitson KS, McNeill LA, Riordan MV, Tian YM, Bullock AN, Welford RW, Elkins JM, Oldham NJ, Bhattacharya S, Gleadle JM, Ratcliffe PJ, Pugh CW, Schofield CJ
TitleHypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family.
[11]
PubMed ID15005628
JournalBiochemistry
Year2004
Volume43
Pages2926-34
AuthorsRoux C, Lee JH, Jeffery CJ, Salmon L
TitleInhibition of type I and type II phosphomannose isomerases by the reaction intermediate analogue 5-phospho-D-arabinonohydroxamic acid supports a catalytic role for the metal cofactor.

comments
Comparing the active site of this enzyme with its homologous enzyme (PDB, 1qwr), conserved Glu294 and Lys136 may act as catalytic residues, and Gln111 may be displaced by substrate binding.
The catalytic cofactor, zinc ion, is bound to two oxygen atoms of substrate, O1 & O2. This enzyme catalyzes two successive isomerization (shift of double-bond position) (see [4], [6] & [11]).
(A) Isomerization (shift of double-bond position; from O=C-C to O-C=C):
(A1) A general base abstract a proton from C2 atom (single-bonded atom). Considering the active-site, Glu294 may acts as the base. This reaction leads to the formation of ene-diol intermediate, forming a double-bond between C1 and C2 atoms. Tyr287 may modulate the function of Glu294 through a hydrogen bond.
(A2) Lys136 may facilitate proton transfer from O2 atom to O1 atom as base-acid, along with zinc ion.
(B) Isomerization (shift of double-bond position; from C=C-O to C-C=O):
(B1) A general acid protonates to C1 atom (double-bonded atom) (from Si face). Considering the active-site, Glu294 may acts as the acid. Tyr287 may modulate the function of Glu294 through a hydrogen bond.

createdupdated
2005-05-272009-02-26


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