HOME
login
history
all enzymes
BRENDA home
History
Information on EC 5.3.1.16 - 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase
for references in articles please use BRENDA:EC5.3.1.16Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
5.3.1.16 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomeraseIUBMB Comments
Involved in histidine biosynthesis.
Specify your search results
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
thisa, bbm ii isomerase, phosphoribosyl-5-amino-1-phosphoribosyl-4-imidazolecarboxamide isomerase, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, bbmii isomerase, profar isomerase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ketol-isomerase
-
-
-
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase
HisA
N'-[(5'-phosphoribosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide isomerase
-
phosphoribosyl-5-amino-1-phosphoribosyl-4-imidazolecarboxamide isomerase
-
ProFAR isomerase
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase
-
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase
-
-
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
Amadori rearrangement
-
1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
enzyme catalyzes Amadori rearrangement of a thermolabile aminoaldolase into the corresponding aminoketose, reaction mechanism involving general acid-base catalysis and a Schiff base intermediate is proposed
-
1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
enzyme catalyzes Amadori rearrangement of a thermolabile aminoaldolase into the corresponding aminoketose, reaction mechanism involving general acid-base catalysis and a Schiff base intermediate is proposed
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide aldose-ketose-isomerase
Involved in histidine biosynthesis.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37318-43-7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-carboxamide
N-(5'-Phospho-D-ribosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
?
-
enzyme catalyzes the fourth step in histidine biosynthesis
-
?
N-(5'-Phospho-D-ribosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
N-(5'-Phospho-D-1-ribulosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-carboxamide
the enzyme catalyzes the fourth step of the His biosynthetic pathway
-
?
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-carboxamide
ProFAR, aminoaldose
PRFAR, aminoketose
r
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
?
-
-
-
?
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
?
-
-
-
?
N-(5'-Phospho-D-ribosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
N-(5'-Phospho-D-1-ribulosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
-
-
-
?
N-(5'-Phospho-D-ribosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
N-(5'-Phospho-D-1-ribulosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
-
-
-
?
additional information
?
-
APG10 knockout mutant exhibits embryo lethality, indicating the essential role of the Arabidopsis BBMII isomerase for plant growth
-
?
additional information
?
-
-
APG10 knockout mutant exhibits embryo lethality, indicating the essential role of the Arabidopsis BBMII isomerase for plant growth
-
?
additional information
?
-
-
enzyme catalyzes Amadori rearrangements of a thermolabile aminoaldolase into the corresponding aminoketose, reaction mechanism involving general acid-base catalysis and a Schiff base intermediate is poposed
-
?
additional information
?
-
-
the enzyme is involved in histidine biosynthesis
-
?
additional information
?
-
-
bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24
-
?
additional information
?
-
-
bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24 has a dual function in both histidine and aromatic amino acid biosynthesis
-
?
additional information
?
-
-
bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24
-
?
additional information
?
-
-
bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24 has a dual function in both histidine and aromatic amino acid biosynthesis
-
?
additional information
?
-
-
bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24
-
?
additional information
?
-
-
bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24 has a dual function in both histidine and aromatic amino acid biosynthesis
-
?
additional information
?
-
-
the enzyme is involved in histidine biosynthesis
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-carboxamide
the enzyme catalyzes the fourth step of the His biosynthetic pathway
-
?
N-(5'-Phospho-D-ribosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
?
-
enzyme catalyzes the fourth step in histidine biosynthesis
-
-
?
1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
?
1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
?
additional information
?
-
APG10 knockout mutant exhibits embryo lethality, indicating the essential role of the Arabidopsis BBMII isomerase for plant growth
-
-
?
additional information
?
-
-
APG10 knockout mutant exhibits embryo lethality, indicating the essential role of the Arabidopsis BBMII isomerase for plant growth
-
-
?
additional information
?
-
-
the enzyme is involved in histidine biosynthesis
-
?
additional information
?
-
-
bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24 has a dual function in both histidine and aromatic amino acid biosynthesis
-
?
additional information
?
-
-
bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24 has a dual function in both histidine and aromatic amino acid biosynthesis
-
?
additional information
?
-
-
bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24 has a dual function in both histidine and aromatic amino acid biosynthesis
-
?
additional information
?
-
-
the enzyme is involved in histidine biosynthesis
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6 - 37.9
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
additional information
additional information
-
Km-values for phosphoribosylanthranilate of mutant enzymes D127V, D127K, D127T, D127G, D127F and D127V/T164H
-
0.6
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25°C or 37°C, pH 7.5, wild-type enzyme
1.6
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25°C, pH 7.5
1.8
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
37°C, pH 7.5
2
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25°C, pH 7.5, mutant enzyme D127N
2.9
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25°C, pH 7.5, mutant enzyme H48A
5.6
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25°C, pH 7.5, mutant enzyme T164A
6.4
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25°C, pH 7.5, mutant enzyme D51N
37.9
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25°C, pH 7.5, mutant enzyme R83N
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00027 - 32
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
additional information
additional information
-
turnover-numbers for phosphoribosylanthranilate of mutant enzymes D127V, D127K, D127T, D127G, D127F and D127V/T164H
-
0.00027
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25°C, pH 7.5, mutant enzyme D127N
0.018
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25°C, pH 7.5, mutant enzyme T164A
0.23
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25°C, pH 7.5, mutant enzyme R83N
0.29
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25°C, pH 7.5, mutant enzyme D51N
0.38
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25°C, pH 7.5, mutant enzyme H48A
0.67
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25°C, pH 7.5, wild-type enzyme
1.54
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
37°C, pH 7.5, wild-type enzyme
2.94
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
37°C, pH 7.5, wild-type enzyme
4.9
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25°C, pH 7.5
6.08
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25°C, pH 7.5, wild-type enzyme
14.3
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
37°C, pH 7.5
32
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
80°C, pH 7.5, wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
catalytic mechanism involves long loops on the catayltic face that enclose the substrate. Substrate ProFAR adopts an extended conformation where its non-reacting half is in a product-like conformation. This change is associated with shifts in a hydrogen bond network including residues His47, Asp129, Thr171, and Ser202
physiological function
-
catalytic mechanism involves long loops on the catayltic face that enclose the substrate. Substrate ProFAR adopts an extended conformation where its non-reacting half is in a product-like conformation. This change is associated with shifts in a hydrogen bond network including residues His47, Asp129, Thr171, and Ser202
Show AA Sequence and Transmembrane Helices (30144 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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25700
-
1 * 25700, equilibrium centrifugation of carboxymethlated enzyme in 8 M urea
28400 - 29500
-
equilibrium centrifugation
29000
-
high speed equilibrium centrifugation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
-
1 * 25700, equilibrium centrifugation of carboxymethlated enzyme in 8 M urea
monomer
-
1 * 29000, high speed equilibrium centrifugation of the enzyme after complete reduction and alkylation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using the anomalous diffraction signal of the protein’s sulfur atoms, enzyme binds a citrate molecule, putative mechanism for the isomerization reaction
wild type in its apo-state and mutants D7N and D7N/D176A in complex with two different conformations of the labile substrate N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide, i.e. ProFAR. Residue D7 acts as the catalytic base, and D176 acts as the catalytic acid
hanging drop vapor diffusion method. All four crystal forms display distinct habits and crystallographic parameters
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D7N
residue D7 acts as the catalytic base, crystallization data
D7N/D176A
residue D7 acts as the catalytic base, and D176 acts as the catalytic acid, crystallization data
D7N
-
residue D7 acts as the catalytic base, crystallization data
D7N/D176A
-
residue D7 acts as the catalytic base, and D176 acts as the catalytic acid, crystallization data
D127N
-
turnover number for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 2481fold higher than that of the wild-type enzyme. The Km-value for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 3.3fold higher than that of the wild-type enzyme
D127V/T164H
-
mutation generates phosporibosylanthranilate isomerase activity
D51N
-
turnover number for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 2.3fold higher than that of the wild-type enzyme. The Km-value for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 9.4fold higher than that of the wild-type enzyme
D8N
-
activity with N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is immeasurable low
H48A
-
turnover number for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 1.8fold lower than that of the wild-type enzyme. The Km-value for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 4.8fold lower than that of the wild-type enzyme
R83N
-
turnover number for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 2.9fold higher than that of the wild-type enzyme. The Km-value for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 63.2fold higher than that of the wild-type enzyme
T164A
-
turnover number for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 37.2fold higher than that of the wild-type enzyme. The Km-value for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 9.3fold higher than that of the wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the gene complements both hisA and trpF mutants of Escherichia coli
the gene complements both hisA and trpF mutants of Escherichia coli
-
the gene complements both hisA and trpF mutants of Escherichia coli
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Martin, R.G.; Berberich, M.A.; Ames, B.N.; Davis, W.W.; Goldberger, R.F.; Yourno, J.D.
Enzymes and intermediates of histidine biosynthesis in Salmonella typhimurium
Methods Enzymol.
17B
3-44
1971
Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Margolies, M.N.; Goldberger, R.F.
Physical and chemical characterization of the isomerase of histidine biosynthesis in Salmonella typhimurium
J. Biol. Chem.
242
256-264
1967
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Margolies, M.N.; Goldberger, R.F.
Isolation of the fourth enzyme (isomerase) of histidine biosynthesis from Salmonella typhimurium
J. Biol. Chem.
241
3262-3269
1966
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Henn-Sax, M.; Thoma, R.; Schmidt, S.; Hennig, M.; Kirschner, K.; Sterner, R.
Two (betaalpha)8-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substrates
Biochemistry
41
12032-12042
2002
Escherichia coli, Thermotoga maritima
brenda
Barona-Gomez, F.; Hodgson, D.A.
Occurrence of a putative ancient-like isomerase involved in histidine and tryptophan biosynthesis
EMBO Rep.
4
296-300
2003
Mycobacterium tuberculosis, Streptomyces coelicolor, Mycobacterium tuberculosis HR37Rv
brenda
Thoma, R.; Obmolova, G.; Lang, D.A.; Schwander, M.; Jeno, P.; Sterner, R.; Wilmanns, M.
Efficient expression, purification and crystallisation of two hyperthermostable enzymes of histidine biosynthesis
FEBS Lett.
454
1-6
1999
Thermotoga maritima
brenda
Fujimori, K.; Tada, S.; Kanai, S.; Ohta, D.
Molecular cloning and characterization of the gene encoding N'-[(5'-phosphoribosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (BBM II) isomerase from Arabidopsis thaliana
Mol. Gen. Genet.
259
216-223
1998
Arabidopsis thaliana (O82782), Arabidopsis thaliana
brenda
Leopoldseder, S.; Claren, J.; Jurgens, C.; Sterner, R.
Interconverting the catalytic activities of (betaalpha)(8)-barrel enzymes from different metabolic pathways: sequence requirements and molecular analysis
J. Mol. Biol.
337
871-879
2004
Thermotoga maritima
brenda
Noutoshi, Y.; Ito, T.; Shinozaki, K.
Albino and pale green 10 encodes BBMII isomerase involved in histidine biosynthesis in Arabidopsis thaliana
Plant Cell Physiol.
46
1165-1172
2005
Arabidopsis thaliana (Q5TKS8), Arabidopsis thaliana
brenda
Quevillon-Cheruel, S.; Leulliot, N.; Graille, M.; Blondeau, K.; Janin, J.; van Tilbeurgh, H.
Crystal structure of the yeast His6 enzyme suggests a reaction mechanism
Protein Sci.
15
1516-1521
2006
Saccharomyces cerevisiae (P40545), Saccharomyces cerevisiae
brenda
Koenigsknecht, M.J.; Lambrecht, J.A.; Fenlon, L.A.; Downs, D.M.
Perturbations in histidine biosynthesis uncover robustness in the metabolic network of Salmonella enterica
PLoS ONE
7
e48207
2012
Salmonella enterica, Salmonella enterica DM10374
brenda
Soederholm, A.; Guo, X.; Newton, M.S.; Evans, G.B.; Naesvall, J.; Patrick, W.M.; Selmer, M.
Two-step ligand binding in a (betaalpha)8 barrel enzyme Substrate-bound structures shed new light on the catalytic cycle of HisA
J. Biol. Chem.
290
24657-24668
2015
Salmonella enterica subsp. enterica serovar Typhimurium (P10372), Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 (P10372)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 5.3.1.16)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
