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Information on EC 2.4.2.17 - ATP phosphoribosyltransferase
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2.4.2.17 ATP phosphoribosyltransferaseIUBMB Comments
Involved in histidine biosynthesis.
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Word Map
- 2.4.2.17
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hisgs
- l-histidine
- glutamicum
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hexameric
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hetero-octameric
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histidyl-trna
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short-form
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long-form
- drug development
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
1-(5-phospho-D-ribosyl)-ATP:pyrophosphate phospho-alpha-D-ribosyltransferase, adenosine 5'-triphosphate phosphoribosyltransferase, adenosine triphosphate phosphoribosyltransferase, adenosine-triphosphate phosphoribosyltransferase, ATP phosphoribosyl transferase, ATP phosphoribosyl transferase complex, ATP phosphoribosyltransferase, ATP-phosphoribosyl transferase, ATP-phosphoribosyltransferase, ATP-PRT, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-(5-phospho-D-ribosyl)-ATP:pyrophosphate phospho-alpha-D-ribosyltransferase
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adenosine 5'-triphosphate phosphoribosyltransferase
adenosine triphosphate phosphoribosyltransferase
ATP phosphoribosyl transferase
ATP phosphoribosyltransferase
ATP-phosphoribosyl transferase
ATP-phosphoribosyltransferase
ATP-PRT
ATP-PRT1
ATP-PRTase
ATPPRT
HisG
HisGL
phosphoribosyl ATP synthetase
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phosphoribosyl ATP:pyrophosphate phosphoribosyltransferase
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phosphoribosyl-ATP pyrophosphorylase
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phosphoribosyl-ATP:pyrophosphate-phosphoribosyl phosphotransferase
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phosphoribosyladenosine triphosphate pyrophosphorylase
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phosphoribosyladenosine triphosphate synthetase
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phosphoribosyltransferase, adenosine triphosphate
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adenosine 5'-triphosphate phosphoribosyltransferase
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adenosine triphosphate phosphoribosyltransferase
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ATP-PRT
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
sequential kinetic mechanism in biosynthetic direction, ordered bi-bi mechanism with ATP binding first to free enzyme and phosphoribosyl-ATP dissociating last from enzyme-product complexes
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1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
sequential kinetic mechanism in biosynthetic direction, ordered bi-bi mechanism with ATP binding first to free enzyme and phosphoribosyl-ATP dissociating last from enzyme-product complexes
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1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
double displacement mechanism
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1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
substrate binding sites, active site structure, switch between active and inactive conformation
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1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
substrate binding sites, e.g. Cys104, Asn75, Ser154, Glu156, and Val155, reaction mechanism
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
1-(5-phospho-D-ribosyl)-ATP:diphosphate phospho-alpha-D-ribosyl-transferase
Involved in histidine biosynthesis.
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CAS REGISTRY NUMBER
COMMENTARY
9031-46-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-alpha-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
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-
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r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
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-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
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-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
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-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
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-
-
?
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
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-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
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-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
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-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
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-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-alpha-D-ribosyl)-ATP + diphosphate
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-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-alpha-D-ribosyl)-ATP + diphosphate
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-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-alpha-D-ribosyl)-ATP + diphosphate
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-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
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-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
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-
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r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
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-
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r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
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-
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r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
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-
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r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
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-
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r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
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-
-
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r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
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-
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r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
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r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
first enzyme in histidine biosynthetic pathway. ATP-PRT expression plays a major role in regulating the pool of free His and contributes to the exceptional Ni tolerance of hyperaccumulator Alyssum species
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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-
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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-
-
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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-
-
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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-
-
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r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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-
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
first step in histidine biosynthesis, enzyme is regulated in a complex allosterical manner, it is a key enzyme is control of the metabolic flux through the pathway
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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first step in histidine biosynthesis
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r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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first reaction of histidine biosynthesis
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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-
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r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
-
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
-
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
first enzyme in histidine biosynthetic pathway. ATP-PRT expression plays a major role in regulating the pool of free His and contributes to the exceptional Ni tolerance of hyperaccumulator Alyssum species
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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first enzyme in histidine biosynthetic pathway. ATP-PRT expression plays a major role in regulating the pool of free His and contributes to the exceptional Ni tolerance of hyperaccumulator Alyssum species
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-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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-
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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-
-
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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-
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r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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-
-
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r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
-
-
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r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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first step in histidine biosynthesis, mechanism of regulation, overview
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-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
first step in histidine biosynthesis
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
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first step in histidine biosynthesis
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
-
first step in histidine biosynthesis
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
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-
-
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
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first step in histidine biosynthesis
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
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-
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r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
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-
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r
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
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-
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r
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
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r
additional information
?
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the enzyme comprises 4 catalytic subunits HisGs and 4 regulatory subunits HisZ with histidine as a ligand, 8 histidine binding sites at the subunit interfaces
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?
additional information
?
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not: ribose 5-phosphate, AMP, ADP, UTP, CTP, GTP
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?
additional information
?
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not: ribose 5-phosphate, AMP, ADP, UTP, CTP, GTP
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?
additional information
?
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not: ribose 5-phosphate, AMP, ADP, UTP, CTP, GTP
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?
additional information
?
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the enzyme comprises 4 catalytic subunits HisGs and 4 regulatory subunits HisZ, only the complete hetero-octameric complex is catalytically active, the complex possesses 8 histidine binding sites at the subunit interfaces and histidine as a ligand
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
first enzyme in histidine biosynthetic pathway. ATP-PRT expression plays a major role in regulating the pool of free His and contributes to the exceptional Ni tolerance of hyperaccumulator Alyssum species
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
first step in histidine biosynthesis, enzyme is regulated in a complex allosterical manner, it is a key enzyme is control of the metabolic flux through the pathway
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
first step in histidine biosynthesis
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
first reaction of histidine biosynthesis
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
first enzyme in histidine biosynthetic pathway. ATP-PRT expression plays a major role in regulating the pool of free His and contributes to the exceptional Ni tolerance of hyperaccumulator Alyssum species
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
first enzyme in histidine biosynthetic pathway. ATP-PRT expression plays a major role in regulating the pool of free His and contributes to the exceptional Ni tolerance of hyperaccumulator Alyssum species
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
first step in histidine biosynthesis, mechanism of regulation, overview
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
first step in histidine biosynthesis
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
-
first step in histidine biosynthesis
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
-
first step in histidine biosynthesis
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
-
-
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
-
first step in histidine biosynthesis
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
replacement of Mg2+ by Mn2+ enhances catalysis by subunit HisGS but not by the holoenzyme
additional information
-
maximal activity is achieved when the concentration of free magnesium reaches about 2 mM, concentrations higher than 5 mM lead to inhibition perhaps due to the formation of MgATP2- complex
Mg2+
-
magnesium could have an effect on the conformation of the enzyme and its activity which would be independent of the state of substrate complexation
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(4E)-4-[(4-chlorophenyl)(hydroxy)methylidene]-1-(pyridin-3-ylmethyl)-5-(3,4,5-trimethoxyphenyl)pyrrolidine-2,3-dione
binds to the cavity between the domains I and II. The terminal chlorobenzoyl group of 1 makes hydrophobic interactions with the amphiphilic pocket near the phosphoribosyl pyrophosphate binding site
1-(5-phospho-alpha-D-ribosyl)-ATP
-
product inhibition, competitive to both substrates
1-[(5,6-diphenyl-1,2,4-triazin-3-yl)sulfanyl]-3-(1,3-thiazol-2-yl)propan-2-one
most potent inhibitor, spans the PR-ATP binding site, exhibits greater than 50% inhibition at 0.01 mM, 40% inhibition at 0.001 mM
4-methoxybenzyl 2-methyl-5-oxo-4,7-dithiophen-2-yl-1,4,5,6,7,8-hexahydroquinoline-3-carboxylate
interacts with the phosphoribosyl diphosphate binding site but less strongly compared to compound 6 , exhibits greater than 50% inhibition at 0.01 mM
5-phospho-alpha-D-ribose 1-diphosphate
-
noncompetitive inhibitor with respect to both substrates in the reaction producing ATP and 5-phospho-alpha-D-ribose 1-diphosphate
adenine
-
competitive to ATP and 5-phospho-alpha-D-ribose 1-diphosphate
beta,gamma-methylene-ATP
-
competitive with respect to N-1-(5-phosphoribosyl)-ATP, noncompetitive with respect to diphosphate; inhibitor of the reaction producing ATP and 5-phospho-alpha-D-ribose 1-diphosphate
dicoumarol
-
competitive with respect to ATP, inhibitor in both directions, diminishes yield of phosphoribosyladenosine triphosphate by acting as parasite substrate
dinitrophenol
-
diminishes yield of phosphoribosyladenosine triphosphate by acting as parasite substrate
diphosphate
-
non competitive to both substrates
ethyl [(6-nitro-1,3-benzothiazol-2-yl)amino](oxo)acetate
exhibits 39% inhibition
Guanosine 5'-diphosphate-3'-diphosphate
-
in presence of partially inhibiting concentrations of histidine guanosine 5'-diphosphate-3'-diphosphate becomes a potent inhibitor of the residual activity of ATP phosphoribosyltransferase, no inhibition in absence of histidine, inhibition is slowly reversible
N-[3-[(6-nitro-1,3-benzothiazol-2-yl)amino]-3-oxo-1-phenylpropyl]benzamide
occupies only the phosphoribosyl diphosphate binding site, exhibits greater than 50% inhibition at 0.01 mM, 35% inhibition at 0.001 mM
Pentachlorophenol
-
competitive to ATP, inhibitor in both directions, diminishes yield of phosphoribosyladenosine triphosphate by acting as parasite substrate
additional information
-
carbonylcyanide m-chlorophenylhydrazone, which is a potent inhibitor of several enzymes with adenine-containing substrates or coenzymes has no effect
-
2-([7-[(3-hydroxyphenyl)amino]-4-nitro-2,1,3-benzoxadiazol-5-yl]amino)-5-nitrophenol
exhibits 46% inhibition
2-([7-[(3-hydroxyphenyl)amino]-4-nitro-2,1,3-benzoxadiazol-5-yl]amino)-5-nitrophenol
-
has whole-cell activity at 0.012 mM
2-[(2-bromo-3,5-dinitrophenyl)carbonyl]-N-phenylhydrazinecarboxamide
exhibits 71% inhibition
2-[(2-bromo-3,5-dinitrophenyl)carbonyl]-N-phenylhydrazinecarboxamide
-
has whole-cell activity at 0.025 mM
ADP
-
competitive to ATP, in the presence of histidine inhibition by AMP and ADP becomes positively cooperative and much more potent
AMP
-
linear competitive inhibitor with respect to ATP, stabilizes the enzyme to thermal inactivation, protect the ordered enzymatic structure against thermodenaturation
AMP
-
competitive inhibitor to 5-phospho-alpha-D-ribose 1-diphosphate, in the presence of histidine inhibition by AMP and ADP becomes positively cooperative and much more potent
histidine
-
feedback inhibition, inhibits the enzyme complex together with ATP to the T-state, no inhibition of mutants E130A and Y268F/Y269F
L-histidine
complete inhibition at 1 mM, about 10% inhibition at 0.25 mM
L-histidine
noncompetitive, alkaline pH decreases the inhibitory effect
L-histidine
-
feed-back inhibition; stabilizes the enzyme to thermal inactivation, protects the ordered enzymatic structure against thermodenaturation, no interaction with binding sites
L-histidine
-
feed-back inhibition; stabilizes the enzyme to thermal inactivation, protects the ordered enzymatic structure against thermodenaturation, no interaction with binding sites
L-histidine
-
allosteric inhibition, synergistically favored by AMP; feed-back inhibition
L-histidine
-
allosteric inhibitor, inhibition dependent on pH, uncompetitive versus ATP, noncompetitive versus 5-phospho-alpha-D-ribosyl diphosphate
L-histidine
in the presence of histidine, subunit HisZ mediates allosteric inhibition of the enzyme
L-histidine
-
feed-back inhibition; reversed by Hg2+, p-hydroxymercuribenzoate, methylmercuric bromide, Ni2+; the L-configuration is essential, substitution of alpha-amino group appreciably reduces inhibition, non competitive inhibitor with respect to both substrates
L-histidine
-
feed-back inhibition
L-histidine
-
feed-back inhibition; inhibits reverse reaction cooperatively and completely
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
potassium chloride
-
stimulates ATP-PRT activity in crude extracts, adding KCl to a final concentration of 0.13 M in reaction mixture increases the reaction rate by about 40%
additional information
-
other salts like ammonium sulfate or ammonium chloride show the same effect as KCl
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis.
Tuberculosis
Discovery of novel nitrobenzothiazole inhibitors for Mycobacterium tuberculosis ATP phosphoribosyl transferase (HisG) through virtual screening.
Tuberculosis
The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition.
Tuberculosis
Transition State Analysis of Adenosine Triphosphate Phosphoribosyltransferase.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.015
5-phospho-alpha-D-ribose 1-diphosphate
wild type long-form enzyme, at pH 8.5 and 25°C
0.0184
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, wild-type enzyme
0.028
5-phospho-alpha-D-ribose 1-diphosphate
truncated long-form enzyme devoid of its regulatory domain, at pH 8.5 and 25°C
0.067
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.07
5-phospho-alpha-D-ribose 1-diphosphate
A270P mutant protein, pH 8.5, temperature not specified in the publication
0.0712
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme D155A
0.08
5-phospho-alpha-D-ribose 1-diphosphate
N215K mutant protein, pH 8.5, temperature not specified in the publication
0.08
5-phospho-alpha-D-ribose 1-diphosphate
N215K/L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
0.08
5-phospho-alpha-D-ribose 1-diphosphate
wild type protein, pH 8.5, temperature not specified in the publication
0.09
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme K8A
0.09
5-phospho-alpha-D-ribose 1-diphosphate
L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
0.13
5-phospho-alpha-D-ribose 1-diphosphate
recombinant At-ATP-PRT1
0.901
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme T162A
0.94
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme K50A
5.15
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme T159A
0.117
ATP
truncated long-form enzyme devoid of its regulatory domain, at pH 8.5 and 25°C
0.22
ATP
N215K mutant protein, pH 8.5, temperature not specified in the publication
0.22
ATP
wild type protein, pH 8.5, temperature not specified in the publication
0.23
ATP
N215K/L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
0.24
ATP
A270P mutant protein, pH 8.5, temperature not specified in the publication
0.35
ATP
L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme K50A
0.024
5-phospho-alpha-D-ribose 1-diphosphate
truncated long-form enzyme devoid of its regulatory domain, at pH 8.5 and 25°C
0.45
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 10°C
0.64
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 15°C
0.84
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme T162A
0.94
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 30°C
0.94
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 20°C
1.07
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme K8A
1.16
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 25°C
1.2
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme T159A
1.29
5-phospho-alpha-D-ribose 1-diphosphate
A270P mutant protein, pH 8.5, temperature not specified in the publication
1.36
5-phospho-alpha-D-ribose 1-diphosphate
L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
1.75
5-phospho-alpha-D-ribose 1-diphosphate
N215K/L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
1.8
5-phospho-alpha-D-ribose 1-diphosphate
wild type long-form enzyme, at pH 8.5 and 25°C
1.91
5-phospho-alpha-D-ribose 1-diphosphate
wild type protein, pH 8.5, temperature not specified in the publication
2.22
5-phospho-alpha-D-ribose 1-diphosphate
N215K mutant protein, pH 8.5, temperature not specified in the publication
2.7
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, wild-type enzyme
2.83
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme D155A
6.16
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme K50A
0.024
ATP
truncated long-form enzyme devoid of its regulatory domain, at pH 8.5 and 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.75
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 10°C
0.86
5-phospho-alpha-D-ribose 1-diphosphate
truncated long-form enzyme devoid of its regulatory domain, at pH 8.5 and 25°C
0.915
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 15°C
1.175
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 30°C
1.266
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 20°C
1.657
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 25°C
120
5-phospho-alpha-D-ribose 1-diphosphate
wild type long-form enzyme , at pH 8.5 and 25°C
0.21
ATP
truncated long-form enzyme devoid of its regulatory domain, at pH 8.5 and 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
1-[(5,6-diphenyl-1,2,4-triazin-3-yl)sulfanyl]-3-(1,3-thiazol-2-yl)propan-2-one
-
0.88
ADP
wild type protein, pH 8.5, temperature not specified in the publication
0.002
N-[3-[(6-nitro-1,3-benzothiazol-2-yl)amino]-3-oxo-1-phenylpropyl]benzamide
-
0.382
AMP
with respect to 5-phospho-alpha-D-ribose 1-diphosphate, at pH 8.5 and 25°C
1.29
AMP
wild type protein, pH 8.5, temperature not specified in the publication
0.0235
L-histidine
-
Kii-value, non competitive versus 5-phospho-alpha-D-ribosyl diphosphate, pH 8.5, 25°C
0.0257
L-histidine
-
Kis-value, non competitive versus 5-phospho-alpha-D-ribosyl diphosphate, pH 8.5, 25°C
0.04
L-histidine
with respect to 5-phospho-alpha-D-ribose 1-diphosphate, at pH 8.5 and 25°C
0.11
L-histidine
wild type protein, pH 8.5, temperature not specified in the publication
0.178
L-histidine
mutant enzyme S232Y/A270D, at pH 8.5 and 30°C
0.24
L-histidine
A270P mutant protein, pH 8.5, temperature not specified in the publication
0.28
L-histidine
N215K mutant protein, pH 8.5, temperature not specified in the publication
0.52
L-histidine
L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
4.15
L-histidine
N215K/L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0119
(4E)-4-[(4-chlorophenyl)(hydroxy)methylidene]-1-(pyridin-3-ylmethyl)-5-(3,4,5-trimethoxyphenyl)pyrrolidine-2,3-dione
Mycobacterium tuberculosis
-
0.004
1-[(5,6-diphenyl-1,2,4-triazin-3-yl)sulfanyl]-3-(1,3-thiazol-2-yl)propan-2-one
Mycobacterium tuberculosis
-
0.0139
2-[(2-bromo-3,5-dinitrophenyl)carbonyl]-N-phenylhydrazinecarboxamide
Mycobacterium tuberculosis
-
0.0055
4-methoxybenzyl 2-methyl-5-oxo-4,7-dithiophen-2-yl-1,4,5,6,7,8-hexahydroquinoline-3-carboxylate
Mycobacterium tuberculosis
-
0.006
N-[3-[(6-nitro-1,3-benzothiazol-2-yl)amino]-3-oxo-1-phenylpropyl]benzamide
Mycobacterium tuberculosis
-
0.0068
1-(5-phospho-beta-D-ribosyl)-ATP
Campylobacter jejuni
truncated long-form enzyme devoid of its regulatory domain, at pH 8.5 and 25°C
0.04
1-(5-phospho-beta-D-ribosyl)-ATP
Campylobacter jejuni
wild type long-form enzyme, at pH 8.5 and 25°C
0.079
AMP
Psychrobacter arcticus
subunit HisGS, at 20°C, pH not specified in the publication
0.42
AMP
Campylobacter jejuni
truncated long-form enzyme devoid of its regulatory domain, at pH 8.5 and 25°C
0.0061
L-histidine
Medicago truncatula
in the presence of 2 mM AMP, at pH 8.0 and 24°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.39
N215K/L231F/T235A/A270P mutant protein, pH 8.5, temperature not specified in the publication
1.96
A270P mutant protein, pH 8.5, temperature not specified in the publication
2.01
N215K mutant protein, pH 8.5, temperature not specified in the publication
2.04
L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
2.1
N215K/L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
2.19
wild type protein, pH 8.5, temperature not specified in the publication
additional information
additional information
-
data for genetically-modified Corynebacterium glutamicum
additional information
-
description of assay method
additional information
-
description of assay method
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 13
>40% relative activity, rapid loss of activity below pH 7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
transcript levels is constitutively higher in Alyssum lesbiacum (a plant that hyperaccumulates Ni and exhibits an exceptional degree of Ni tolerance) than in the congeneric nonaccumulator Alyssum montanum, transcript levels in the weak hyperaccumulator Alyssum serpyllifolium is intermediate
brenda
transcript levels is constitutively higher in Alyssum lesbiacum (a plant that hyperaccumulates Ni and exhibits an exceptional degree of Ni tolerance) than in the congeneric nonaccumulator Alyssum montanum, transcript levels in the weak hyperaccumulator Alyssum serpyllifolium is intermediate
brenda
-
transcript levels is constitutively higher in Alyssum lesbiacum (a plant that hyperaccumulates Ni and exhibits an exceptional degree of Ni tolerance) than in the congeneric nonaccumulator Alyssum montanum, transcript levels in the weak hyperaccumulator Alyssum serpyllifolium is intermediate
brenda
transcript levels is constitutively higher in Alyssum lesbiacum (a plant that hyperaccumulates Ni and exhibits an exceptional degree of Ni tolerance) than in the congeneric nonaccumulator Alyssum montanum, transcript levels in the weak hyperaccumulator Alyssum serpyllifolium is intermediate
brenda
transcript levels is constitutively higher in Alyssum lesbiacum (a plant that hyperaccumulates Ni and exhibits an exceptional degree of Ni tolerance) than in the congeneric nonaccumulator Alyssum montanum, transcript levels in the weak hyperaccumulator Alyssum serpyllifolium is intermediate
brenda
-
transcript levels is constitutively higher in Alyssum lesbiacum (a plant that hyperaccumulates Ni and exhibits an exceptional degree of Ni tolerance) than in the congeneric nonaccumulator Alyssum montanum, transcript levels in the weak hyperaccumulator Alyssum serpyllifolium is intermediate
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Show AA Sequence and Transmembrane Helices (36548 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
210000 - 221000
-
sedimentation, equilibrium centrifugation with meniscus depletion method
216000
-
ultracentrifugation analysis
25308
truncated long-form enzyme devoid of its regulatory domain, calculated from amino acid sequence
32191
33000
-
6 * 33000, SDS-disc gel electrophoresis
36000
-
6 * 36000, viscometric methods, equilibrium centrifugation with meniscus depletion method after dialysis against 5.0 M guanidine-HCl and 0.143 M 2-mercaptoethanol
32191
2 * 32191, MALDI-TOF MS, gel filtration, theoretical molecular mass 31000
32191
6 * 32191, MALDI-TOF MS, gel filtration, theoretical molecular mass 31000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterooctamer
hexamer
homodimer
2 * 32191, MALDI-TOF MS, gel filtration, theoretical molecular mass 31000
homohexamer
homohexamer or heterooctamer
octamer
additional information
heterooctamer
4 * 40000 + 4 * 23000, subunits HisZ and HisGS, SDS-PAGE
heterooctamer
short-form ATP phosphoribosyltransferase is a hetero-octameric allosteric enzyme comprising four catalytic subunits (HisGS) and four regulatory subunits (HisZ)
heterooctamer
the enzyme consist of four catalytic subunits (HisGS) and four regulatory subunits (HisZ)
heterooctamer
-
the enzyme consist of four catalytic subunits (HisGS) and four regulatory subunits (HisZ)
-
heterooctamer
-
4 * 40000 + 4 * 23000, subunits HisZ and HisGS, SDS-PAGE
-
heterooctamer
-
short-form ATP phosphoribosyltransferase is a hetero-octameric allosteric enzyme comprising four catalytic subunits (HisGS) and four regulatory subunits (HisZ)
-
hexamer
-
6 * 36000, viscometric methods, equilibrium centrifugation with meniscus depletion method after dialysis against 5.0 M guanidine-HCl and 0.143 M 2-mercaptoethanol
hexamer
-
6 * 33000, SDS-disc gel electrophoresis
homohexamer
6 * 32191, MALDI-TOF MS, gel filtration, theoretical molecular mass 31000
homohexamer
-
6 * 31515.1, ESI-MS, gel filtration, His-tagged protein, not influenced by allosteric inhibitor L-histidine or ATP
homohexamer
-
6 * 31515.1, ESI-MS, gel filtration, His-tagged protein, not influenced by allosteric inhibitor L-histidine or ATP
-
homohexamer or heterooctamer
the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine
homohexamer or heterooctamer
-
the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine
-
homohexamer or heterooctamer
the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine
homohexamer or heterooctamer
the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine
homohexamer or heterooctamer
-
the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine
-
octamer
-
4 * catalytic subunit HisGs + 4 * regulatory subunit HisZ, (alpha,beta)4
octamer
-
four HisGS catalytic subunits related to periplasmic binding proteins and four HisZ regulatory subunits that resemble histidyl-tRNA synthetases
octamer
-
4 * catalytic subunit HisGs + 4 * regulatory subunit HisZ, (alpha,beta)4
additional information
-
overall structure and monomer architecture, several motif 2 loops in both subunit types, switch structure between active and inactive conformation
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with ATP, L-histidine, or L-histidine/AMP, hanging drop vapor diffusion method, using 0.1M sodium acetate, 0.1 M MgCl2, 13-15% (w/v) PEG 4000, pH 5.5 (ATP), or 0.1 M BTP, 0.2 M KSCN, 13-14% (w/v) PEG 3350, pH 6.5 (His), or 0.1 M Tris, 0.1 M MgCl2, 13-15% (w/v) PEG 4000, pH 7.5 (L-His/AMP)
truncated long-form enzyme devoid of its regulatory domain as apoenzyme and in complex with ATP, 5-phospho-alpha-D-ribose 1-diphosphate or 1-(5-phospho-beta-D-ribosyl)-ATP, hanging drop vapor diffusion method, using 1 M sodium acetate, 10 mM ZnCl2, and 7-10% (w/v) PEG 6000 (pH 5.0)
purified recombinant selenomethionine-labeled enzyme in complex with inhibitor AMP or with product 1-(5-phospho-D-ribosyl)-ATP, X-ray diffraction enzyme-inhibitor complex structure determination and analysis at 2.7 A resolution, X-ray diffraction enzyme-product complex structure determination and analysis at 2.9 A resolution, modeling
vapour diffusion method, trigonal prisms are obtained using 1.3 M sodium tartrate, 50-200 mM magnesium chloride, 100 mM citrate buffer pH 5.6 and enzyme in the presence of 2 mM AMP, round shaped crystals are obtained with 1.36-1.44 M ammonium sulfate, 0-0.3 M sodium chloride, 100 mM HEPES buffer pH 7.5 and enzyme in the presence of 2 mM AMP
-
purified recombinant wild-type and selenomethionine-labeled enzyme complex, the latter additionally by microseeding, hanging drop vapour diffusion method, 0.002 ml well solution containing 15-25% v/v PEG 400, 0.1 M Tris-HCl, pH 7.5, 0.2 M MgCl2, mixed with equal volume of protein solution containing 10-16 mg/ml protein, 10 mM ATP, or 10 mM N-1-methyl-ATP and 5 mM 5-phospho-alpha-D-ribose 1-diphosphate, crystal growth is dependent on ATP or N-1-methyl-ATP, derivatization with 2.5 mM sodium tungstate dihydrate, cryoprotection with 17-18% glycerol, X-ray diffraction structure determination and analysis at 2.9-3.2 A resolution
-
native and SeMet-labeled enzyme, hanging drop vapor diffusion method, using 2.53 M NaCl, 100 mM Bis-Tris propane pH 6.3, and 10% (v/v) glycerol
hanging drop vapour diffusion method at 16°C, the apocrystals are obtained using 0.1 M buffer MES pH 6.5 and magnesium sulfate as precipitant, crystals in the presence of AMP and histidine are obtained using 0.1 M sodium citrate pH 5.6, 0.5 M ammonium sulfate and 1 M lithium sulfate with 5 mM AMP and 0.1 mM histidine
-
hanging drop vapor diffusion method, using 11% (w/v) PEG 3350, 0.1 M bicine (pH 8.5), 0.15 M SrCl2, 0.15 M KBr, and 2% (v/v) 1,6-hexanediol
holoenzyme and catalytic subunit HisGS in complexes with substrates (5-phospho-alpha-D-ribose 1-diphosphate, 5-phospho-alpha-D-ribose 1-diphosphate-ATP, 5-phospho-alpha-D-ribose 1-diphosphate-ADP), product (N1-(5-phospho-beta-D-ribosyl)-ATP) and inhibitor (AMP), hanging drop vapor diffusion method, using 10% (w/v) polyethylene glycol 3350, 0.1 M bicine pH 8.5, 50 mM MgCl2, 0.1 M KBr, and 4% (v/v) 1,6-hexanediol
purified recombinant wild-type and selenomethionine-labeled subunits HisGs and HisZ separately, in a binary complex with histidine, sitting drop vapour diffusion method, 0.002 ml of 8 mg/ml protein mixed with 0.002 ml reservoir solution containing 22.5% w/v methyl-2,4-pentanediol, 0.2 M phosphate/citrate buffer, pH 4.2, 2 days, X-ray diffraction structure determination and analysis at 2.5 A resolution, modeling
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R216A
the mutant shows more than 50% inhibition at 0.25 mM AMP and complete loss of response to histidine while retaining its histidine-binding ability
R216Q
the mutant shows about 50% inhibition at 0.25 mM AMP, about 20% inhibition at 0.025 mM L-histidine, and about 45% inhibition at 0.25 mM ATP plus 0.025 mM L-histidine
R216A
-
the mutant shows more than 50% inhibition at 0.25 mM AMP and complete loss of response to histidine while retaining its histidine-binding ability
-
R216Q
-
the mutant shows about 50% inhibition at 0.25 mM AMP, about 20% inhibition at 0.025 mM L-histidine, and about 45% inhibition at 0.25 mM ATP plus 0.025 mM L-histidine
-
A249T
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
A270D
the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme
D213N
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
G230S
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
N215K/L231F/T235A
conserved residues, 37fold increase in Ki-value of histidine
S143F
the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme
S232Y
the mutant with increased activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme
S232Y/A270D
the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme
T228P
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
T235M
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
D213N
-
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
-
G230S
-
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
-
S143F
-
the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme
-
T235M
-
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
-
D155A
-
slight increase in kcat, 3.9fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 1.7fold increase in Km-value for ATP
E130A
-
site-directed mutagenesis, about 60% reduced activity compared to the wild-type enzyme, no inhibition by histidine
K50A
-
2.3fold increase in kcat, 51fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 1.8fold increase in Km-value for ATP
K8A
-
2.5fold decrease in kcat, 4.9fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 3.1fold increase in Km-value for ATP
T159A
-
2.2fold decrease in kcat, 280fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 2.5fold decrease in Km-value for ATP
T162A
-
3.2fold decrease in kcat, 49fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 2.6fold decrease in Km-value for ATP
Y268F/Y269F
-
site-directed mutagenesis, about 30% reduced activity compared to the wild-type enzyme, no inhibition by histidine
additional information
additional information
deletion of the entire C-terminal regulatory domain in combination with the gain of function mutation S143F in the catalytic domain results in an enzyme variant that is still highly active even at L-histidine concentrations close to the solubility limit
additional information
-
deletion of the entire C-terminal regulatory domain in combination with the gain of function mutation S143F in the catalytic domain results in an enzyme variant that is still highly active even at L-histidine concentrations close to the solubility limit
additional information
-
deletion of the entire C-terminal regulatory domain in combination with the gain of function mutation S143F in the catalytic domain results in an enzyme variant that is still highly active even at L-histidine concentrations close to the solubility limit
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
overview: stability at various pH-values
637669
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
very sensitive to heat inactivation, 0.4 mM histidine stabilizes the enzyme to inactivation by heat
47.5
-
1.9 mg enzyme/ml, 80 min, 75% loss of activity without addition of AMP, with 0.05 mM AMP about 60% loss of activity, with 0.5 mM AMP about 40% loss of activity, with 5 mM AMP about 25% loss of activity
48
-
3 mg enzyme/ml, 10 min, 15% remaining activity without addition of histidine, with 0.000086 mM histidine about 15% remaining activity after 15 min, with 0.00069 mM histidine about 70% remaining activity after 80 min, with 0.00345 mM histidine about 80% remaining activity after 80 min, with 0.0069 mM histidine about 55% remaining activity after 50 min
52.5
melting temperature of the truncated long-form enzyme devoid of its regulatory domain
additional information
-
heat inactivation depends on protein concentration and inhibitors
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
histidine or AMP stabilizes the enzyme with respect to thermal inactivation
-
L-histidine, 0.4 mM, stabilizes against heat inactivation, 0.04 mM does not stabilize against heat inactivation, at 1.33 mM and higher heat inactivation is greater than the control
-
NaCl and 2-mercaptoethanol stabilize the very labile enzyme
-
overview, stability of the enzyme at various pH-values, salt concentrations and histidine concentrations
-
slight stabilization by 10 mM MgCl2 or CaCl2 by 1 mM MnCl2 and by 1 mM histidine at pH-values above 7
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM Tris-HCl, pH 7.5, 0.4 mM DTT and one protease inhibitor per litre, 50% v/v glycerol, long term storage
-
4°C, 0.01 M Tris, 0.10 M NaCl, 0.4 mM histidine, 2.8 mM 2-mercaptoethanol, 0.5 mM EDTA, pH 7.5, 50% loss of activity after several days
-
4°C, HEPES buffer pH 7.5, final ammonium sulfate microcrystalline enzyme in 60% saturated ammonium sulfate, 0.1 M NaCl, 0.01 M Tris, 1.5 mM EDTA, 10 mM dithiothreitol, stable for 1 month, greater than 95% activity retained
-
storage in liquid nitrogen of quick-frozen enzyme in HEPES buffer pH 7.5, 0.1 M NaCl, 0.01 M Tris, 0.5 mM EDTA, 1 mM dithiothreitol, 1 mM histidine, indefinitely stable, preserves 100% activity. The critical factor for stability seems to be the maintenance of a sulfhydryl-reducing environment, high dithiothreitol concentrations has no adverse effect at either 0°C or 37°C
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and DEAE-cellulose chromatography
-
first purification by heating the crude extract, ammonium sulfate precipitation and selective histidine-dependent ammonium sulfate precipitation
-
HisTrap resin column chromatography and Superdex S200 gel filtration
HiTrap Talon column chromatography and Superdex 200 gel filtration
HiTrap Talon resin column chromatography, GST-affinity column chromatography and Superdex S200 gel filtration
immobilized metal ion affinity chromatography, gel filtration
metal affinity column chromatography
metal affinity column chromatography and Sephacryl S-200 gel filtration
Mn2+ precipitation, DEAE-cellulose and ammonium sulfate precipitation, later on Sephadex G-150
-
recombinant wild-type and selenomethionine-labeled enzyme complex comprising subunits HisGs and HisZ from Escherichia coli
-
recombinant wild-type and selenomethionine-labeled subunits HisGs and HisZ from Escherichia coli in a multistep procedure
-
the recombinant enzymes are produced as fused proteins with a maltose-binding protein, and the purification is made by a two step amylose resin column followed by a digestion with Factor Xa
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
codon adapted to Escherichia coli, synthetically prepared, His-tagged protein expressed in Escherichia coli BL21(DE3)pLysS
-
expressed in Escherichia coli BL21(DE3) cells
overexpression of an Alyssum lesbiacum ATP-PRT cDNA in transgenic Arabidopsis thaliana increases the pool of free His up to 15fold in shoot tissue, without affecting the concentration of any other amino acid. His-overproducing lines also display elevated tolerance to Ni but do not exhibit increased Ni concentrations in either xylem sap or shoot tissue, suggesting that additional factors are necessary to recapitulate the complete hyperaccumulator phenotype
overexpression of subunits HisGs and HisZ comprising complex in Escherichia coli strain BL21(DE3) as wild-type, or in strain B834 as selenomethionine-labeled complex
-
separate expression of subunits HisGs and HisZ in Escherichia coli strain BL21(DE3) as wild-type, or in strain B834 as selenomethionine-labeled proteins
-
overexpression of an Alyssum lesbiacum ATP-PRT cDNA in transgenic Arabidopsis thaliana increases the pool of free His up to 15fold in shoot tissue, without affecting the concentration of any other amino acid. His-overproducing lines also display elevated tolerance to Ni but do not exhibit increased Ni concentrations in either xylem sap or shoot tissue, suggesting that additional factors are necessary to recapitulate the complete hyperaccumulator phenotype
overexpression of an Alyssum lesbiacum ATP-PRT cDNA in transgenic Arabidopsis thaliana increases the pool of free His up to 15fold in shoot tissue, without affecting the concentration of any other amino acid. His-overproducing lines also display elevated tolerance to Ni but do not exhibit increased Ni concentrations in either xylem sap or shoot tissue, suggesting that additional factors are necessary to recapitulate the complete hyperaccumulator phenotype
overexpression of an Alyssum lesbiacum ATP-PRT cDNA in transgenic Arabidopsis thaliana increases the pool of free His up to 15fold in shoot tissue, without affecting the concentration of any other amino acid. His-overproducing lines also display elevated tolerance to Ni but do not exhibit increased Ni concentrations in either xylem sap or shoot tissue, suggesting that additional factors are necessary to recapitulate the complete hyperaccumulator phenotype
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
forced histidine exposure (through injection or feeding) significantly inhibits the enzyme mRNA levels at higher concentrations
-
histidine exposure significantly increases enzyme expression levels at lower concentrations (feeding only)
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
drug development
-
HisG represents a potential drug target for tuberculosis
drug development
HisG represents a potential drug target for tuberculosis
drug development
-
HisG represents a potential drug target for tuberculosis
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Martin, R.G.
The first enzyme in histidine biosynthesis: the nature of feedback inhibition by histidine
J. Biol. Chem.
238
257-268
1963
Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Tebar, A.R.; Ballesteros, A.O.
Kinetic properties of ATP phosphoribosyltransferase of Escherichia coli
Mol. Cell. Biochem.
11
131-136
1976
Escherichia coli
brenda
Ames, B.N.; Martin, R.G.; Garry, B.J.
The first step in histidine biosynthesis
J. Biol. Chem.
236
2019-2026
1961
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Voll, M.J.; Appella, E.; Martin, R.G.
Purification and composition studies of phosphoribosyladenosine triphosphate:pyrophosphate phosphoribosyltransferase, the first enzyme of histidine biosynthesis
J. Biol. Chem.
242
1760-1767
1967
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Morton, D.P.; Parsons, S.M.
Synergistic inhibition of ATP phosphoribosyltransferase by guanosine tetraphosphate and histidine
Biochem. Biophys. Res. Commun.
74
172-177
1977
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Morton, D.P.; Parsons, S.M.
Inhibition of ATP phosphoribosyltransferase by AMP and ADP in the absence and presence of histidine
Arch. Biochem. Biophys.
181
643-648
1977
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Dall-Larsen, T.; Kryvi, H.; Klungsoyr, L.
Dinitrophenol, dicoumarol and pentachlorophenol as inhibitors and parasite substrates in the ATP phosphoribosyltransferase reaction
Eur. J. Biochem.
66
443-446
1976
Escherichia coli
brenda
Kryvi, H.
Thermal stability of phosphoribosyladenosine triphosphate synthetase as reflected in its circular dichroism and activity properties. Effect of inhibitors
Biochim. Biophys. Acta
317
123-130
1973
Escherichia coli
brenda
Parsons, S.M.; Koshland, D.E.
A rapid isolation of phosphoribosyladenosine triphosphate synthetase and comparison to native enzyme
J. Biol. Chem.
249
4104-4109
1974
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Morton, D.P.; Parsons, S.M.
Biosynthetic direction substrate kinetics and product inhibition studies on the first enzyme of histidine biosynthesis, adenosine triphosphate phosphoribosyltransferase
Arch. Biochem. Biophys.
175
677-686
1976
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Kleeman, J.E.; Parsons, S.M.
Reverse direction substrate kinetics and inhibition studies on the first enzyme of histidine biosynthesis, adenosine triphosphate phosphoribosyltransferase
Arch. Biochem. Biophys.
175
687-693
1976
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Mizukami, T.; Hamu, A.; Ideka, M.; Oka, T.; Katsumata, R.
Cloning of the ATP phosphoribosyl transferase gene of Corynebacterium glutamicum and application of the gene to L-histidine production
Biosci. Biotechnol. Biochem.
58
635-638
1994
Corynebacterium glutamicum
brenda
Ohta, D.; Fujimori, K.; Mizutani, M.; Nakayama, Y.; Kunpaisal-Hashimoto, R.; Munzer, S.; Kozaki, A.
Molecular cloning and characterization of ATP-phosphoribosyl transferase from Arabidopsis, a key enzyme in the histidine biosynthetic pathway
Plant Physiol.
122
907-914
2000
Arabidopsis thaliana, Arabidopsis thaliana (Q9S762)
brenda
Lohkamp, B.; Coggins, J.R.; Lapthorn, A.J.
Purification, crystallization and preliminary x-ray crystallographic analysis of ATP-phosphoribosyltransferase from Escherichia coli
Acta Crystallogr. Sect. D
56
1488-1491
2000
Escherichia coli
brenda
Cho, Y.; Sharma, V.; Sacchettini, J.C.
Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis
J. Biol. Chem.
278
8333-8339
2003
Mycobacterium tuberculosis
brenda
Champagne, K.S.; Sissler, M.; Larrabee, Y.; Doublie, S.; Francklyn, C.S.
Activation of the hetero-octameric ATP phosphoribosyl transferase through subunit interface rearrangement by a tRNA synthetase paralog
J. Biol. Chem.
280
34096-34104
2005
Lactococcus lactis
brenda
Lohkamp, B.; McDermott, G.; Campbell, S.A.; Coggins, J.R.; Lapthorn, A.J.
The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition
J. Mol. Biol.
336
131-144
2004
Escherichia coli (P60757), Escherichia coli
brenda
Vega, M.C.; Zou, P.; Fernandez, F.J.; Murphy, G.E.; Sterner, R.; Popov, A.; Wilmanns, M.
Regulation of the hetero-octameric ATP phosphoribosyl transferase complex from Thermotoga maritima by a tRNA synthetase-like subunit
Mol. Microbiol.
55
675-686
2005
Thermotoga maritima
brenda
Champagne, K.S.; Piscitelli, E.; Francklyn, C.S.
Substrate recognition by the hetero-octameric ATP phosphoribosyltransferase from Lactococcus lactis
Biochemistry
45
14933-14943
2006
Lactococcus lactis
brenda
Ingle, R.A.; Mugford, S.T.; Rees, J.D.; Campbell, M.M.; Smith, J.A.
Constitutively high expression of the histidine biosynthetic pathway contributes to nickel tolerance in hyperaccumulator plants
Plant Cell
17
2089-2106
2005
Odontarrhena serpyllifolia, Alyssum montanum (Q56US5), Alyssum montanum, Odontarrhena lesbiaca (Q56UT2), Odontarrhena lesbiaca (Q56UT3), Odontarrhena lesbiaca
brenda
Cho, Y.; Ioerger, T.R.; Sacchettini, J.C.
Discovery of novel nitrobenzothiazole inhibitors for Mycobacterium tuberculosis ATP phosphoribosyl transferase (HisG) through virtual screening
J. Med. Chem.
51
5984-5992
2008
Mycobacterium tuberculosis (P9WMN1), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WMN1), Mycolicibacterium smegmatis
brenda
Pedreno, S.; Pisco, J.P.; Larrouy-Maumus, G.; Kelly, G.; de Carvalho, L.P.
Mechanism of feedback allosteric inhibition of ATP phosphoribosyltransferase
Biochemistry
51
8027-8038
2012
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Zhang, Y.; Shang, X.; Deng, A.; Chai, X.; Lai, S.; Zhang, G.; Wen, T.
Genetic and biochemical characterization of Corynebacterium glutamicum ATP phosphoribosyltransferase and its three mutants resistant to feedback inhibition by histidine
Biochimie
94
829-838
2012
Corynebacterium glutamicum (Q9Z472), Corynebacterium glutamicum
brenda
Kulis-Horn, R.K.; Persicke, M.; Kalinowski, J.
Corynebacterium glutamicum ATP-phosphoribosyl transferases suitable for L-histidine production - Strategies for the elimination of feedback inhibition
J. Biotechnol.
206
26-37
2015
Corynebacterium glutamicum (Q9Z472), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q9Z472)
brenda
Mittelstaedt, G.; Moggre, G.J.; Panjikar, S.; Nazmi, A.R.; Parker, E.J.
Campylobacter jejuni adenosine triphosphate phosphoribosyltransferase is an active hexamer which is allosterically controlled by the twisting of a regulatory tail
Protein Sci.
25
1492-1506
2016
Campylobacter jejuni (Q9PM78), Campylobacter jejuni, Campylobacter jejuni NCTC 11168 (Q9PM78)
brenda
Alphey, M.; Fisher, G.; Ge, Y.; Gould, E.; Machado, T.; Liu, H.; Florence, G.; Naismith, J.; Da Silva, R.
Catalytic and anticatalytic snapshots of a short-form ATP phosphoribosyltransferase
ACS Catal.
8
5601-5610
2018
Psychrobacter arcticus (Q4FQF7), Psychrobacter arcticus DSM 17307 (Q4FQF7)
-
brenda
Moggre, G.J.; Poulin, M.B.; Tyler, P.C.; Schramm, V.L.; Parker, E.J.
Transition state analysis of adenosine triphosphate phosphoribosyltransferase
ACS Chem. Biol.
12
2662-2670
2017
Mycobacterium tuberculosis (P9WMN1), Mycobacterium tuberculosis, Lactococcus lactis (Q02129), Lactococcus lactis, Campylobacter jejuni (Q5HSJ4), Campylobacter jejuni, Mycobacterium tuberculosis H37Rv (P9WMN1), Campylobacter jejuni RM1221 (Q5HSJ4)
brenda
Wan, P.J.; Tang, Y.H.; Yuan, S.Y.; Wang, W.X.; Lai, F.X.; Yu, X.P.; Fu, Q.
ATP phosphoribosyltransferase from symbiont Entomomyces delphacidicola invovled in histidine biosynthesis of Nilaparvata lugens (Stal)
Amino Acids
48
2605-2617
2016
Nilaparvata lugens
brenda
Mittelstaedt, G.; Jiao, W.; Livingstone, E.K.; Moggre, G.J.; Nazmi, A.R.; Parker, E.J.
A dimeric catalytic core relates the short and long forms of ATP-phosphoribosyltransferase
Biochem. J.
475
247-260
2018
Campylobacter jejuni (Q5HSJ4), Campylobacter jejuni RM 1221 (Q5HSJ4)
brenda
Ruszkowski, M.
Guarding the gateway to histidine biosynthesis in plants Medicago truncatula ATP-phosphoribosyltransferase in relaxed and tense states
Biochem. J.
475
2681-2697
2018
Medicago truncatula (G7JFL4), Medicago truncatula
brenda
Stroek, R.; Ge, Y.; Talbot, P.D.; Glok, M.K.; Bernas, K.E.; Thomson, C.M.; Gould, E.R.; Alphey, M.S.; Liu, H.; Florence, G.J.; Naismith, J.H.; da Silva, R.G.
Kinetics and structure of a cold-adapted hetero-octameric ATP phosphoribosyltransferase
Biochemistry
56
793-803
2017
Psychrobacter arcticus (Q4FQF7), Psychrobacter arcticus DSM 17307 (Q4FQF7)
brenda
Fisher, G.; Thomson, C.M.; Stroek, R.; Czekster, C.M.; Hirschi, J.S.; da Silva, R.G.
Allosteric activation shifts the rate-limiting step in a short-form ATP phosphoribosyltransferase
Biochemistry
57
4357-4367
2018
Psychrobacter arcticus (Q4FQF7), Psychrobacter arcticus DSM 17307 (Q4FQF7)
brenda
Jiao, W.; Mittelstaedt, G.; Moggre, G.J.; Parker, E.J.
Hinge twists and population shifts deliver regulated catalysis for ATP-PRT in histidine biosynthesis
Biophys. J.
116
1887-1897
2019
Campylobacter jejuni (Q5HSJ4), Campylobacter jejuni RM1221 (Q5HSJ4)
brenda
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