DB code: T00095

CATH domain 1.10.275.10 : Fumarase C; Chain B, domain 1 Catalytic domain
1.20.200.10 : Fumarase C; Chain A, domain 2 Catalytic domain
1.10.40.30 : Ribonucleotide Reductase Protein R1; domain 1
E.C. 4.3.2.2
CSA 1c3c
M-CSA 1c3c
MACiE M0080

CATH domain Related DB codes (homologues)
1.10.275.10 : Fumarase C; Chain B, domain 1 D00267 T00086 T00092 T00094
1.10.40.30 : Ribonucleotide Reductase Protein R1; domain 1 T00086 T00092 T00094
1.20.200.10 : Fumarase C; Chain A, domain 2 D00267 T00086 T00092 T00094

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
Q8ZY28
Adenylosuccinate lyase (PurB)
NP_558986.1 (Protein)
NC_003364.1 (DNA/RNA sequence)
PF00206 (Lyase_1)
[Graphical View]
Q9X0I0 Adenylosuccinate lyase
ASL
EC 4.3.2.2
Adenylosuccinase
ASase
NP_228901.1 (Protein)
NC_000853.1 (DNA/RNA sequence)
PF10397 (ADSL_C)
PF00206 (Lyase_1)
[Graphical View]

KEGG enzyme name
adenylosuccinate lyase
adenylosuccinase
succino AMP-lyase
6-N-(1,2-dicarboxyethyl)AMP AMP-lyase
6-N-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q8ZY28 Q8ZY28_PYRAE
Q9X0I0 PUR8_THEMA N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP. (S)-2-(5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1- (5-phospho-D-ribosyl)imidazole-4-carboxamide.

KEGG Pathways
Map code Pathways E.C.
MAP00230 Purine metabolism
MAP00252 Alanine and aspartate metabolism

Compound table
Substrates Products Intermediates
KEGG-id C03794 C04823 C00122 C00020 C04677
E.C.
Compound N6-(1,2-Dicarboxyethyl)-AMP 1-(5'-Phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole Fumarate AMP 1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide
Type amino acids,carboxyl group,nucleotide amino acids,amide group,amine group,carbohydrate,nucleotide carboxyl group amine group,nucleotide amide group,amine group,nucleotide
ChEBI 18319
 18319
 		18012
 18012
 		16027
 16027
 		18406
 18406
PubChem 447145
 447145
 		160666
 160666
 		21883788
 444972
 21883788
 444972
 		6083
 6083
 		65110
 65110
1dofA01 Unbound Unbound Unbound Unbound Unbound
1dofB01 Unbound Unbound Unbound Unbound Unbound
1dofC01 Unbound Unbound Unbound Unbound Unbound
1dofD01 Unbound Unbound Unbound Unbound Unbound
1c3cA01 Unbound Unbound Unbound Unbound Unbound
1c3cB01 Unbound Unbound Unbound Unbound Unbound
1c3uA01 Unbound Unbound Unbound Unbound Unbound
1c3uB01 Unbound Unbound Unbound Unbound Unbound
1dofA02 Unbound Unbound Unbound Unbound Unbound
1dofB02 Unbound Unbound Unbound Unbound Unbound
1dofC02 Unbound Unbound Unbound Unbound Unbound
1dofD02 Unbound Unbound Unbound Unbound Unbound
1c3cA02 Unbound Unbound Unbound Unbound Unbound
1c3cB02 Unbound Unbound Unbound Unbound Unbound
1c3uA02 Unbound Unbound Unbound Unbound Unbound
1c3uB02 Unbound Unbound Unbound Unbound Unbound
1dofA03 Unbound Unbound Unbound Unbound Unbound
1dofB03 Unbound Unbound Unbound Unbound Unbound
1dofC03 Unbound Unbound Unbound Unbound Unbound
1dofD03 Unbound Unbound Unbound Unbound Unbound
1c3cA03 Unbound Unbound Unbound Unbound Unbound
1c3cB03 Unbound Unbound Unbound Unbound Unbound
1c3uA03 Unbound Unbound Unbound Unbound Unbound
1c3uB03 Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;Q9X0I0 & literature [5] & [9]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1dofA01 HIS 72 invisible 64-71
1dofB01 HIS 72 invisible 64-71
1dofC01 HIS 72 invisible 64-71
1dofD01 HIS 72 invisible 64-71
1c3cA01 HIS 68
1c3cB01 HIS 68
1c3uA01 HIS 68
1c3uB01 HIS 68
1dofA02 HIS 143;GLU 275 invisible 260-268
1dofB02 HIS 143;GLU 275 invisible 260-268
1dofC02 HIS 143;GLU 275 invisible 260-268
1dofD02 HIS 143;GLU 275 invisible 260-268
1c3cA02 HIS 141;GLU 275
1c3cB02 HIS 141;GLU 275
1c3uA02 HIS 141;GLU 275
1c3uB02 HIS 141;GLU 275
1dofA03
1dofB03
1dofC03
1dofD03
1c3cA03
1c3cB03
1c3uA03
1c3uB03

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig.1, p.660-661
[8]
Fig.5c, p.166-169 2
[9]
p.2224

References
[1]
Resource
Comments
Medline ID
PubMed ID 3759987
Journal J Biol Chem
Year 1986
Volume 261
Pages 13637-42
Authors Casey PJ, Abeles RH, Lowenstein JM
Title Metabolism of threo-beta-fluoroaspartate by H4 cells. Inhibition of adenylosuccinate lyase by fluoro analogs of its substrates.
Related PDB
Related UniProtKB
[2]
Resource
Comments Homologous enzymes
Medline ID
PubMed ID 7552727
Journal Nat Struct Biol
Year 1995
Volume 2
Pages 654-62
Authors Weaver TM, Levitt DG, Donnelly MI, Stevens PP, Banaszak LJ
Title The multisubunit active site of fumarase C from Escherichia coli.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 8969519
Journal Microbiology
Year 1996
Volume 142
Pages 3219-30
Authors Green SM, Malik T, Giles IG, Drabble WT
Title The purB gene of Escherichia coli K-12 is located in an operon.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 8845770
Journal Protein Sci
Year 1996
Volume 5
Pages 786-8
Authors Redinbo MR, Eide SM, Stone RL, Dixon JE, Yeates TO
Title Crystallization and preliminary structural analysis of Bacillus subtilis adenylosuccinate lyase, an enzyme implicated in infantile autism.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 9890879
Journal Biochemistry
Year 1999
Volume 38
Pages 22-32
Authors Lee TT, Worby C, Bao ZQ, Dixon JE, Colman RF
Title His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of Bacillus subtilis.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 11063569
Journal Biochemistry
Year 2000
Volume 39
Pages 13336-43
Authors Brosius JL, Colman RF
Title A key role in catalysis for His89 of adenylosuccinate lyase of Bacillus subtilis.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 10926519
Journal J Mol Biol
Year 2000
Volume 301
Pages 433-50
Authors Toth EA, Worby C, Dixon JE, Goedken ER, Marqusee S, Yeates TO
Title The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds.
Related PDB 1dof
Related UniProtKB
[8]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID 20139703
PubMed ID 10673438
Journal Structure Fold Des
Year 2000
Volume 8
Pages 163-74
Authors Toth EA, Yeates TO
Title The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway.
Related PDB 1c3c 1c3u
Related UniProtKB Q9X0I0
[9]
Resource
Comments
Medline ID
PubMed ID 11841213
Journal Biochemistry
Year 2002
Volume 41
Pages 2217-26
Authors Brosius JL, Colman RF
Title Three subunits contribute amino acids to the active site of tetrameric adenylosuccinate lyase: Lys268 and Glu275 are required.
Related PDB
Related UniProtKB

Comments
This enzyme catalyzes two similar reactions, in which fumarate will be cut from nucleotide derivatives. The active site and catalytic mechanism seem to be shared by these reactions.

Created Updated
2004-06-28 2009-04-03