The enzyme which converts 3-phosphoglycerate to 2-phosphglycerate is
O phosphglycerate kinase
phosphglycerate synthase
phosphglycerate mutase
enolase
Answers
Answer:
Phosphoglycerate kinase (EC 2.7.2.3) (PGK 1) is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglycerate (1,3-BPG) to ADP producing 3-phosphoglycerate (3-PG) and ATP :
Phosphoglycerate kinase
Phosphoglycerate kinase 3PGK.png
Identifiers
EC number
2.7.2.3
CAS number
9001-83-6
Databases
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB structures
RCSB PDB PDBe PDBsum
Gene Ontology
AmiGO / QuickGO
Search
PMC
articles
PubMed
articles
NCBI
proteins
Phosphoglycerate kinase
PDB 3pgk EBI.jpg
Structure of yeast phosphoglycerate kinase.[1]
Identifiers
Symbol
PGK
Pfam
PF00162
InterPro
IPR001576
PROSITE
PDOC00102
SCOPe
3pgk / SUPFAM
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
1,3-bisphosphoglycerate + ADP ⇌ glycerate 3-phosphate + ATP
Like all kinases it is a transferase. PGK is a major enzyme used in glycolysis, in the first ATP-generating step of the glycolytic pathway. In gluconeogenesis, the reaction catalyzed by PGK proceeds in the opposite direction, generating ADP and 1,3-BPG.
In humans, two isozymes of PGK have been so far identified, PGK1 and PGK2. The isozymes have 87-88% identical amino acid sequence identity and though they are structurally and functionally similar, they have different localizations: PGK2, encoded by an autosomal gene, is unique to meiotic and postmeiotic spermatogenic cells, while PGK1, encoded on the X-chromosome, is ubiquitously expressed in all cells.[2]
Explanation:
Phosphoglycerate kinase (EC 2.7.2.3) (PGK 1) is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglycerate (1,3-BPG) to ADP producing 3-phosphoglycerate (3-PG) and ATP :
Phosphoglycerate kinase
Phosphoglycerate kinase 3PGK.png
Identifiers
EC number
2.7.2.3
CAS number
9001-83-6
Databases
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB structures
RCSB PDB PDBe PDBsum
Gene Ontology
AmiGO / QuickGO
Search
PMC
articles
PubMed
articles
NCBI
proteins
Phosphoglycerate kinase
PDB 3pgk EBI.jpg
Structure of yeast phosphoglycerate kinase.[1]
Identifiers
Symbol
PGK
Pfam
PF00162
InterPro
IPR001576
PROSITE
PDOC00102
SCOPe
3pgk / SUPFAM
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
1,3-bisphosphoglycerate + ADP ⇌ glycerate 3-phosphate + ATP
Like all kinases it is a transferase. PGK is a major enzyme used in glycolysis, in the first ATP-generating step of the glycolytic pathway. In gluconeogenesis, the reaction catalyzed by PGK proceeds in the opposite direction, generating ADP and 1,3-BPG.
In humans, two isozymes of PGK have been so far identified, PGK1 and PGK2. The isozymes have 87-88% identical amino acid sequence identity and though they are structurally and functionally similar, they have different localizations: PGK2, encoded by an autosomal gene, is unique to meiotic and postmeiotic spermatogenic cells, while PGK1, encoded on the X-chromosome, is ubiquitously expressed in all cells.[2]
Answer:
phosphoglycerate mutase