EzCatDB: S00391

DB codeS00391
CATH domainDomain 13.40.225.10Catalytic domain
E.C.4.1.2.17
CSA1fua
MACiEM0072


Enzyme Name
Swiss-protKEGG

P0AB87
Protein nameL-fuculose phosphate aldolaseL-fuculose-phosphate aldolase
L-fuculose 1-phosphate aldolase
fuculose aldolase
L-fuculose-1-phosphate lactaldehyde-lyase
SynonymsEC 4.1.2.17
L-fuculose-1-phosphate aldolase

KEGG pathways
MAP codePathways
MAP00051Fructose and mannose metabolism

Swiss-prot:Accession NumberP0AB87
Entry nameFUCA_ECOLI
ActivityL-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde.
SubunitHomotetramer.
Subcellular location
CofactorBinds 1 zinc ion per subunit.


CofactorsSubstratesProducts
KEGG-idC00038C01099C00111C00424
CompoundZincL-Fuculose 1-phosphateGlycerone phosphate(S)-Lactaldehyde
Typeheavy metalcarbohydrate,phosphate group/phosphate ioncarbohydrate,phosphate group/phosphate ioncarbohydrate
1dzuPBound:_ZNUnboundUnboundUnbound
1dzvPBound:_ZNUnboundUnboundUnbound
1dzwPBound:_ZNUnboundUnboundUnbound
1dzxPBound:_ZNUnboundUnboundUnbound
1dzyPBound:_ZNUnboundUnboundUnbound
1dzzPBound:_ZNUnboundUnboundUnbound
1e46PBound:_ZNUnboundUnboundUnbound
1e47PBound:_ZNUnboundBound:13PUnbound
1e48PBound:_ZNUnboundBound:13PUnbound
1e49PBound:_ZNUnboundUnboundUnbound
1e4aPBound:_ZNUnboundUnboundUnbound
1e4bPBound:_ZNUnboundUnboundUnbound
1e4cPBound:_ZNUnboundUnboundUnbound
1fuaABound:_ZNUnboundUnboundUnbound
2fuaAAnalogue:_COUnboundUnboundUnbound
3fuaABound:_ZNUnboundUnboundUnbound
4fuaABound:_ZNUnboundAnalogue:PGHUnbound

Active-site residues
resource
Swiss-prot;P0AB87 & literature;[3],[5]
pdbCatalytic residuesCofactor-binding residuescomment
1dzuPGLU 73;TYR 113
GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
mutant T26A
1dzvPGLU 73;       
GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
mutant Y113F;Y209F
1dzwPGLU 73;TYR 113
GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
mutant F131A
1dzxPGLU 73;TYR 113
GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
mutant R212A
1dzyPGLU 73;TYR 113
GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
mutant E214A
1dzzPGLU 73;       
GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
mutant Y113F
1e46P      ;TYR 113
      ;HIS 92;HIS 94;HIS 155(Zinc binding)
mutant E73S
1e47P      ;TYR 113
      ;HIS 92;HIS 94;HIS 155(Zinc binding)
mutant E73Q
1e48P      ;       
      ;HIS 92;HIS 94;HIS 155(Zinc binding)
mutant E73Q;Y113F;Y209F
1e49PGLU 73;TYR 113
GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
mutant N29L;S71A
1e4aPGLU 73;TYR 113
GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
deletion A27
1e4bPGLU 73;TYR 113
GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
mutant N29Q
1e4cPGLU 73;TYR 113
GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
mutant S71Q
1fuaAGLU 73;TYR 113
GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)

2fuaAGLU 73;TYR 113
GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)

3fuaAGLU 73;TYR 113
GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)

4fuaAGLU 73;TYR 113
GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Fig.6, p.463-4653
[4]Fig.6, p.57522
[5]Fig.3
[8]Fig.2
[9]Fig.1

references
[1]
PubMed ID8515438
JournalJ Mol Biol
Year1993
Volume231
Pages549-53
AuthorsDreyer MK, Schulz GE
TitleThe spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
JournalActa Crystallogr D Biol Crystallogr
Year1996
Volume52
Pages1082-91
AuthorsDreyer MK, Schulz GE
TitleRefined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli.
Related PDB1fua,2fua
Related Swiss-protP0AB87
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND CATALYTIC MECHANISM.
Medline ID96256522
PubMed ID8676381
JournalJ Mol Biol
Year1996
Volume259
Pages458-66
AuthorsDreyer MK, Schulz GE
TitleCatalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure.
Related PDB3fua,4fua
Related Swiss-protP0AB87
[4]
CommentsHomologous enzyme
PubMed ID9548961
JournalBiochemistry
Year1998
Volume37
Pages5746-54
AuthorsJohnson AE, Tanner ME
TitleEpimerization via carbon-carbon bond cleavage. L-ribulose-5-phosphate 4-epimerase as a masked class II aldolase.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS), AND MUTAGENESIS.
Medline ID20281325
PubMed ID10821675
JournalBiochemistry
Year2000
Volume39
Pages6033-41
AuthorsJoerger AC, Gosse C, Fessner WD, Schulz GE
TitleCatalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis.
Related PDB1dzu,1dzv,1dzw,1dzx,1dzy,1dzz
Related Swiss-protP0AB87
[6]
CommentsHomologous enzyme
PubMed ID10769138
JournalBiochemistry
Year2000
Volume39
Pages4808-20
AuthorsLee LV, Vu MV, Cleland WW
Title13C and deuterium isotope effects suggest an aldol cleavage mechanism for L-ribulose-5-phosphate 4-epimerase.
[7]
CommentsX-RAY CRYSTALLOGRAPHY OF MUTANTS.
Medline ID20510153
PubMed ID11054289
JournalJ Mol Biol
Year2000
Volume303
Pages531-43
AuthorsJoerger AC, Mueller-Dieckmann C, Schulz GE
TitleStructures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis.
Related PDB1e46,1e47,1e48,1e49,1e4a,1e4b,1e4c
Related Swiss-protP0AB87
[8]
CommentsHomologous enzyme
PubMed ID11732895
JournalBiochemistry
Year2001
Volume40
Pages14763-71
AuthorsLuo Y, Samuel J, Mosimann SC, Lee JE, Tanner ME, Strynadka NC
TitleThe structure of L-ribulose-5-phosphate 4-epimerase: an aldolase-like platform for epimerization.
[9]
CommentsHomologous enzyme
PubMed ID11732896
JournalBiochemistry
Year2001
Volume40
Pages14772-80
AuthorsSamuel J, Luo Y, Morgan PM, Strynadka NC, Tanner ME
TitleCatalysis and binding in L-ribulose-5-phosphate 4-epimerase: a comparison with L-fuculose-1-phosphate aldolase.

comments
This enzyme belongs to the aldolase class II family, which utilizes the metal ion as cofactor.

createdupdated
2004-06-282009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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