EzCatDB: T00236

DB codeT00236
CATH domainDomain 13.20.20.240Catalytic domain
Domain 23.90.970.10
Domain 33.40.50.280Catalytic domain
E.C.5.4.99.1
CSA1cb7
MACiEM0063

CATH domainRelated DB codes (homologues)
3.20.20.240M00168
3.40.50.280M00172,M00168

Enzyme Name
Swiss-protKEGG

P80077P80078Q05509Q05488
Protein nameMethylaspartate mutase E chainMethylaspartate mutase S chainMethylaspartate mutase E chainMethylaspartate mutase S chainmethylaspartate mutase
glutamate mutase
glutamic mutase
glutamic isomerase
glutamic acid mutase
glutamic acid isomerase
methylaspartic acid mutase
beta-methylaspartate-glutamate mutase
glutamate isomerase
SynonymsEC 5.4.99.1
Glutamate mutase subunit epsilon
EC 5.4.99.1
Glutamate mutase subunit sigma
EC 5.4.99.1
Glutamate mutase subunit epsilon
EC 5.4.99.1
Glutamate mutase subunit sigma

KEGG pathways
MAP codePathways
MAP00660C5-Branched dibasic acid metabolism

Swiss-prot:Accession NumberP80077P80078Q05509Q05488
Entry nameGLME_CLOCOMAMA_CLOCOGLME_CLOTTMAMA_CLOTT
ActivityL-threo-3-methylaspartate = L-glutamate.L-threo-3-methylaspartate = L-glutamate.L-threo-3-methylaspartate = L-glutamate.L-threo-3-methylaspartate = L-glutamate.
SubunitHeterotetramer of 2 E subunits and 2 S subunits.Heterotetramer of 2 E subunits and 2 S subunits.Possible heterotetramer, composed of two E chains and two S chains. E exists as a homodimer and S as a monomer.Heterotetramer of 2 E subunits and 2 S subunits. E exists as a homodimer and S as a monomer.
Subcellular location



CofactorCobalamin.5''-deoxy-5''-adenosyl-adeninylcobamide (pseudo-coenzyme B12).Cobalamin.5''-deoxy-5''-adenosyl-adeninylcobamide (pseudo-coenzyme B12).


CofactorsSubstratesProducts
KEGG-idC00194C03618C00025
CompoundCobamide coenzymeL-threo-3-MethylaspartateL-Glutamate
Typeamide group,amine group,aromatic ring (with nitrogen atoms),carbohydrate,heavy metal,nucleoside,nucleotideamino acids,carboxyl groupamino acids,carboxyl group
1cb7B01UnboundAnalogue:TARUnbound
1cb7D01UnboundAnalogue:TARUnbound
1ccwB01UnboundAnalogue:TARUnbound
1ccwD01UnboundAnalogue:TARUnbound
1i9cB01Bound:5ADBound:3MDBound:GLU
1i9cD01Bound:5ADBound:3MDBound:GLU
1cb7B02UnboundUnboundUnbound
1cb7D02UnboundUnboundUnbound
1ccwB02UnboundUnboundUnbound
1ccwD02UnboundUnboundUnbound
1i9cB02UnboundUnboundUnbound
1i9cD02UnboundUnboundUnbound
1b1aAUnboundUnboundUnbound
1cb7AAnalogue:COBUnboundUnbound
1cb7CAnalogue:COBUnboundUnbound
1ccwAAnalogue:CNCUnboundUnbound
1ccwCAnalogue:CNCUnboundUnbound
1i9cABound:B12UnboundUnbound
1i9cCBound:B12UnboundUnbound
1be1AUnboundUnboundUnbound
1fmfAUnboundUnboundUnbound
1id8AUnboundUnboundUnbound

Active-site residues
resource
literature [14], [18], [28]
pdbCatalytic residuesCofactor-binding residues
1cb7B01ARG 100;GLU 171

1cb7D01ARG 100;GLU 171

1ccwB01ARG 100;GLU 171

1ccwD01ARG 100;GLU 171

1i9cB01ARG 100;GLU 171

1i9cD01ARG 100;GLU 171

1cb7B02       

1cb7D02       

1ccwB02       

1ccwD02       

1i9cB02       

1i9cD02       

1b1aAASP 14
HIS 16(Cobamide coenzyme binding)
1cb7AASP 14
HIS 16(Cobamide coenzyme binding)
1cb7CASP 14
HIS 16(Cobamide coenzyme binding)
1ccwAASP 14
HIS 16(Cobamide coenzyme binding)
1ccwCASP 14
HIS 16(Cobamide coenzyme binding)
1i9cAASP 14
HIS 16(Cobamide coenzyme binding)
1i9cCASP 14
HIS 16(Cobamide coenzyme binding)
1be1AASP 14
HIS 16(Cobamide coenzyme binding)
1fmfAASP 14
HIS 16(Cobamide coenzyme binding)
1id8AASP 14
HIS 16(Cobamide coenzyme binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[9]Scheme 1, Scheme 2
[10]Fig.2, p.11870-11872
[12]Fig.1
[14]Fig.1, p.897, p.899-900
[15]Fig.5
[16]Scheme 2
[17]Scheme 1
[18]Fig. 1, Fig.5, p.1147-1148
[20]

[25]Fig.4, p.600-601
[26]

[28]Fig.1, p.3243-3245
[29]Fig.1, Fig.4, p.2690-2691

references
[1]
PubMed ID1315276
JournalEur J Biochem
Year1992
Volume205
Pages759-65
AuthorsLeutbecher U, Bocher R, Linder D, Buckel W
TitleGlutamate mutase from Clostridium cochlearium. Purification, cobamide content and stereospecific inhibitors.
[2]
PubMed ID1322827
JournalFEBS Lett
Year1992
Volume307
Pages144-6
AuthorsLeutbecher U, Albracht SP, Buckel W
TitleIdentification of a paramagnetic species as an early intermediate in the coenzyme B12-dependent glutamate mutase reaction. A cob(II)amide?
[3]
PubMed ID7712296
JournalCurr Opin Struct Biol
Year1994
Volume4
Pages919-29
AuthorsDrennan CL, Matthews RG, Ludwig ML
TitleCobalamin-dependent methionine synthase: the structure of a methylcobalamin-binding fragment and implications for other B12-dependent enzymes.
[4]
PubMed ID7880251
JournalEur J Biochem
Year1994
Volume226
Pages577-85
AuthorsZelder O, Beatrix B, Leutbecher U, Buckel W
TitleCharacterization of the coenzyme-B12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli.
[5]
PubMed ID7649266
JournalFEBS Lett
Year1995
Volume369
Pages252-4
AuthorsZelder O, Beatrix B, Kroll F, Buckel W
TitleCoordination of a histidine residue of the protein-component S to the cobalt atom in coenzyme B12-dependent glutamate mutase from Clostridium cochlearium.
[6]
PubMed ID9003368
JournalBiochem J
Year1996
Volume320
Pages825-30
AuthorsHolloway DE, Harding SE, Marsh EN
TitleAdenosylcobalamin-dependent glutamate mutase: properties of a fusion protein in which the cobalamin-binding subunit is linked to the catalytic subunit.
[7]
PubMed ID8910568
JournalJ Biol Chem
Year1996
Volume271
Pages29121-5
AuthorsHolloway DE, Chen HP, Marsh EN
TitleCarboxymethylation of MutS-cysteine-15 specifically inactivates adenosylcobalamin-dependent glutamate mutase. Examination of the role of this residue in coenzyme-binding and catalysis.
[8]
PubMed ID9201933
JournalBiochemistry
Year1997
Volume36
Pages7884-9
AuthorsChen HP, Marsh EN
TitleHow enzymes control the reactivity of adenosylcobalamin: effect on coenzyme binding and catalysis of mutations in the conserved histidine-aspartate pair of glutamate mutase.
[9]
PubMed ID9521732
JournalBiochemistry
Year1998
Volume37
Pages4105-13
AuthorsBothe H, Darley DJ, Albracht SP, Gerfen GJ, Golding BT, Buckel W
TitleIdentification of the 4-glutamyl radical as an intermediate in the carbon skeleton rearrangement catalyzed by coenzyme B12-dependent glutamate mutase from Clostridium cochlearium.
[10]
PubMed ID9718309
JournalBiochemistry
Year1998
Volume37
Pages11864-72
AuthorsMarsh EN, Ballou DP
TitleCoupling of cobalt-carbon bond homolysis and hydrogen atom abstraction in adenosylcobalamin-dependent glutamate mutase.
[11]
CommentsSTRUCTURE BY NMR.
PubMed ID9739092
JournalStructure
Year1998
Volume6
Pages1021-33
AuthorsTollinger M, Konrat R, Hilbert BH, Marsh EN, Krautler B
TitleHow a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum.
Related PDB1be1
Related Swiss-protQ05488
[12]
PubMed ID10521275
JournalBiochemistry
Year1999
Volume38
Pages13684-91
AuthorsChih HW, Marsh EN
TitlePre-steady-state kinetic investigation of intermediates in the reaction catalyzed by adenosylcobalamin-dependent glutamate mutase.
[13]
CommentsNMR spectroscopy
PubMed ID10429202
JournalEur J Biochem
Year1999
Volume263
Pages178-88
AuthorsHoffmann B, Konrat R, Bothe H, Buckel W, Krautler B
TitleStructure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium cochlearium.
Related PDB1b1a
[14]
CommentsX-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
Medline ID99404935
PubMed ID10467146
JournalStructure Fold Des
Year1999
Volume7
Pages891-902
AuthorsReitzer R, Gruber K, Jogl G, Wagner UG, Bothe H, Buckel W, Kratky C
TitleGlutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights.
Related PDB1cb7,1ccw
Related Swiss-protP80077
[15]
PubMed ID10956023
JournalBiochemistry
Year2000
Volume39
Pages10340-6
AuthorsRoymoulik I, Moon N, Dunham WR, Ballou DP, Marsh EN
TitleRearrangement of L-2-hydroxyglutarate to L-threo-3-methylmalate catalyzed by adenosylcobalamin-dependent glutamate mutase.
[16]
CommentsX-ray crystallography
PubMed ID11592143
JournalAngew Chem Int Ed Engl
Year2001
Volume40
Pages3377-3380
AuthorsGruber K, Reitzer R, Kratky C
TitleRadical Shuttling in a Protein: Ribose Pseudorotation Controls Alkyl-Radical Transfer in the Coenzyme B(12) Dependent Enzyme Glutamate Mutase.
Related PDB1i9c
[17]
PubMed ID11256957
JournalBiochem J
Year2001
Volume355
Pages131-7
AuthorsHuhta MS, Chen HP, Hemann C, Hille CR, Marsh EN
TitleProtein-coenzyme interactions in adenosylcobalamin-dependent glutamate mutase.
[18]
PubMed ID11755393
JournalChem Biol
Year2001
Volume8
Pages1143-9
AuthorsMadhavapeddi P, Marsh EN
TitleThe role of the active site glutamate in the rearrangement of glutamate to 3-methylaspartate catalyzed by adenosylcobalamin-dependent glutamate mutase.
[19]
CommentsNMR spectroscopy
PubMed ID11828501
JournalChembiochem
Year2001
Volume2
Pages643-55
AuthorsHoffmann B, Tollinger M, Konrat R, Huhta M, Marsh EN, Krautler B
TitleA protein pre-organized to trap the nucleotide moiety of coenzyme B(12): refined solution structure of the B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum.
Related PDB1fmf
[20]
PubMed ID11506551
JournalJ Am Chem Soc
Year2001
Volume123
Pages7963-72
AuthorsWetmore SD, Smith DM, Golding BT, Radom L
TitleInterconversion of (S)-glutamate and (2S,3S)-3-methylaspartate: a distinctive B(12)-dependent carbon-skeleton rearrangement.
[21]
PubMed ID11727974
JournalJ Biomol NMR
Year2001
Volume21
Pages107-16
AuthorsEichmuller C, Schuler W, Konrat R, Krautler B
TitleSimultaneous measurement of intra- and intermolecular NOEs in differentially labeled protein-ligand complexes.
[22]
PubMed ID11519744
JournalJ Biomol NMR
Year2001
Volume20
Pages195-202
AuthorsEichmuller C, Tollinger M, Krautler B, Konrat R
TitleMapping the ligand binding site at protein side-chains in protein-ligand complexes through NOE difference spectroscopy.
[23]
CommentsNMR spectroscopy
PubMed ID11397096
JournalJ Mol Biol
Year2001
Volume309
Pages777-91
AuthorsTollinger M, Eichmuller C, Konrat R, Huhta MS, Marsh EN, Krautler B
TitleThe B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum traps the nucleotide moiety of coenzyme B(12).
Related PDB1id8
[24]
PubMed ID11863459
JournalBiochemistry
Year2002
Volume41
Pages3200-6
AuthorsHuhta MS, Ciceri D, Golding BT, Marsh EN
TitleA novel reaction between adenosylcobalamin and 2-methyleneglutarate catalyzed by glutamate mutase.
[25]
PubMed ID12413543
JournalCurr Opin Chem Biol
Year2002
Volume6
Pages598-603
AuthorsGruber K, Kratky C
TitleCoenzyme B(12) dependent glutamate mutase.
[26]
PubMed ID12797824
JournalChem Rev
Year2003
Volume103
Pages2083-94
AuthorsBanerjee R
TitleRadical carbon skeleton rearrangements: catalysis by coenzyme B12-dependent mutases.
[27]
PubMed ID14979711
JournalBiochemistry
Year2004
Volume43
Pages2155-8
AuthorsCheng MC, Marsh EN
TitlePre-steady-state measurement of intrinsic secondary tritium isotope effects associated with the homolysis of adenosylcobalamin and the formation of 5'-deoxyadensosine in glutamate mutase.
[28]
PubMed ID15023074
JournalBiochemistry
Year2004
Volume43
Pages3238-45
AuthorsXia L, Ballou DP, Marsh EN
TitleRole of Arg100 in the active site of adenosylcobalamin-dependent glutamate mutase.
[29]
PubMed ID15709782
JournalBiochemistry
Year2005
Volume44
Pages2686-91
AuthorsCheng MC, Marsh EN
TitleIsotope effects for deuterium transfer between substrate and coenzyme in adenosylcobalamin-dependent glutamate mutase.

comments
According to the literature, this enzyme catalyzes "fragmentation" and "recombination" by radical transfer from Cobamide coenzyme (or Vitamine B12).

createdupdated
2005-05-202009-03-10


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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