KEGG   ENZYME: 5.5.1.27Help
Entry
EC 5.5.1.27                 Enzyme                                 

Name
D-galactarolactone cycloisomerase;
GCI
Class
Isomerases;
Intramolecular lyases;
Intramolecular lyases (only sub-subclass identified to date)
BRITE hierarchy
Sysname
D-galactaro-1,4-lactone lyase (ring-opening)
Reaction(IUBMB)
(1) D-galactaro-1,4-lactone = 5-dehydro-4-deoxy-D-glucarate [RN:R10847];
(2) D-glucaro-1,4-lactone = 5-dehydro-4-deoxy-D-glucarate [RN:R11083]
Reaction(KEGG)
Substrate
D-galactaro-1,4-lactone [CPD:C20896];
D-glucaro-1,4-lactone [CPD:C21095]
Product
5-dehydro-4-deoxy-D-glucarate [CPD:C00679]
Comment
The enzyme, characterized from the bacterium Agrobacterium fabrum strain C58, is involved in degradation of D-galacturonate and D-glucuronate. Activity with D-galactaro-1,4-lactone is 4-fold higher than with D-glucaro-1,4-lactone.
History
EC 5.5.1.27 created 2015
Pathway
Ascorbate and aldarate metabolism
Orthology
K18983  
D-galactarolactone cycloisomerase
Genes
CAMA: 
SOD: 
PAO: 
KLN: 
VNI: 
PGB: 
PAT: 
PBW: 
MTHD: 
CSA: 
HEL: 
HAK: 
HAM: 
MME: 
MPC: 
MARS: 
AKA: 
MES: 
RHI: 
SFH: 
EAD: 
ATU: 
ATF: 
ATA: 
AGR: 
RIR: 
NGL: 
NGG: 
BJU: 
BJP: 
BRC: 
BRAD: 
BOP: 
XAU: 
SNO: 
CHEL: 
PHL: 
SIL: 
RDE: 
RLI: 
OAT: 
MALG: 
ABS: 
ABQ: 
BSS: 
BST: 
GYO_1403(yitF)
BAE: 
BATR: 
BLR: 
PNP: 
LPIL: 
SBH: 
SXI: 
AGY: 
PSIM: 
ABAC: 
LuPra_02649(dgoD_3)
PLS: 
CAO: 
CLY: 
CLH: 
CBAL: 
CBAT: 
ZGA: 
HGI: 
NOU: 
HLR: 
VDI: 
 » show all
Taxonomy
Reference
1  [PMID:22493433]
  Authors
Andberg M, Maaheimo H, Boer H, Penttila M, Koivula A, Richard P
  Title
Characterization of a novel Agrobacterium tumefaciens galactarolactone cycloisomerase enzyme for direct conversion of D-galactarolactone to 3-deoxy-2-keto-L-threo-hexarate.
  Journal
J. Biol. Chem. 287 (2012) 17662-71.
  Sequence
[atu:Atu3139]
Reference
2  [PMID:24450804]
  Authors
Bouvier JT, Groninger-Poe FP, Vetting M, Almo SC, Gerlt JA.
  Title
Galactaro delta-lactone isomerase: lactone isomerization by a member of the amidohydrolase superfamily.
  Journal
Biochemistry. 53 (2014) 614-6.
  Sequence
[atu:Atu3139]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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