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Information on EC 3.5.1.5 - urease and Organism(s) Klebsiella aerogenes and UniProt Accession P18315

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.5 urease
IUBMB Comments
A nickel protein.
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This record set is specific for:
Klebsiella aerogenes
UNIPROT: P18315 not found.
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Word Map
The taxonomic range for the selected organisms is: Klebsiella aerogenes
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
+
=
+
2
Synonyms
urease, jack bean urease, canatoxin, acid urease, jbure-ii, embryo-specific soybean urease, urea amidohydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Arthritogenic cationic 19 kDa antigen
-
-
-
-
Urea amidohydrolase
-
-
-
-
urease
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
urea + H2O = CO2 + 2 NH3
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
condensation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
urea amidohydrolase
A nickel protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9002-13-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
urea + H2O
CO2 + 2 NH3
show the reaction diagram
-
-
-
?
urea + H2O
CO2 + NH3
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
urea + H2O
CO2 + 2 NH3
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Nickel
additional information
-
urease apoprotein binds numerous metal ions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
epigallocatechin
strong time-dependent inactivation of urease that is not due to their oxygen sensitivity. Rather, the compound appears to inactivate urease by reacting with a specific Cys residue located on the flexible loop. Substitution of this cysteine by alanine in the C319A variant increases the urease resistance
iodoacetamide
-
phosphate protects wild-type enzyme from inactivation, does not affect inactivation of C319S urease
quercetin
strong time-dependent inactivation of urease that is not due to their oxygen sensitivity. Rather, the compound appears to inactivate urease by reacting with a specific Cys residue located on the flexible loop. Substitution of this cysteine by alanine in the C319A variant increases the urease resistance
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4 - 2090
Urea
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 3500
Urea
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1250
Urea
-
pH 7.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2200
wild type, 2.1 Ni2+/active site
2500
-
pH 7.75, temperature not specified in the publication
440
G11P (UreB), 1.67 Ni2+/active site
690
-
pH 7.5, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
mutant D221A
5.2
-
mutant enzymes C319S and C319D
6
-
mutant enzymes H320A, H320N and H320A
6.7
-
mutant C319A
6.8
-
mutant enzyme alphaH320A
7.6
-
wild-type enzyme
7.8
-
wild-type enzyme
8
-
wild-type enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
about 65% of maximal activity at pH 7.0 and 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
URE3_KLEAE
100
0
11087
Swiss-Prot
-
URE2_KLEAE
106
0
11695
Swiss-Prot
-
URE1_KLEAE
567
0
60305
Swiss-Prot
-
A0A447W5G5_KLEAE
146
0
15847
TrEMBL
-
A0A377RH56_KLEAE
100
0
11087
TrEMBL
-
A0A447W5F4_KLEAE
572
0
60965
TrEMBL
-
A0A447W4X7_KLEAE
567
0
60291
TrEMBL
-
A0A3S4J7K8_KLEAE
106
0
11695
TrEMBL
-
A0A447W5G6_KLEAE
100
0
11065
TrEMBL
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11000
-
alpha2beta4tau4, 2 * 72000 + 4 * 11000 + 4 * 9000, SDS-PAGE
11100
-
gamma subunit, method not specified
11700
-
beta subunit, method not specified
224000
-
gel filtration
60300
-
alpha subunit, method not specified
72000
-
alpha2beta4tau4, 2 * 72000 + 4 * 11000 + 4 * 9000, SDS-PAGE
9000
-
alpha2beta4tau4, 2 * 72000 + 4 * 11000 + 4 * 9000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
-
alpha2beta4tau4, 2 * 72000 + 4 * 11000 + 4 * 9000, SDS-PAGE
trimer
-
composed of three distinct subunits, one large (60 kDa) and two small (11 kDa), commonly forming (alpha beta gamma)3 trimers
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure determined at 2.2 A
-
urease is inactive in the crystalline form, possibly due to conformational restrictions associated with a lid covering the active site
-
wild-type and mutant enzyme
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alphaH134A
-
no detectable activity, 53% of the nickel content of wild-type enzyme
alphaH136A
-
no detectable activity, 6% of the nickel content of wild-type enzyme
alphaH219A
-
1.9% of the activity of the wild-type enzyme, 80% of the nickel content of the wild type enzyme, very high Km-value compared to wild-type enzyme
alphaH246A
-
no detectable activity, 21% of the nickel content of wild-type enzyme
alphaH320A
-
normal nickel content, 0.003% of the activity of the wild-type enzyme, unlike wild-type enzyme no inactivation by diethyldicarbonate
alphaH321A
-
activity and nickel content are similar to wild-type enzyme
betaH39A
-
activity and nickel content are similar to wild-type enzyme
betaH41A
-
activity and nickel content are similar to wild-type enzyme
C319A
C319D
-
0.03% of the activity of the wild-type enzyme, nickel content of the mutant is lower than that of the wild-type enzyme, small increase in Km-value
C319S
-
4.5% of the activity of the wild-type enzyme, nickel content of the mutant is lower than that of the wild-type enzyme, small increase in Km-value
D221A
-
low activity, small increase in Km-value and pH 5 optimum
G11P
UreB, subunit beta, analysis of urease activation
G18P
UreB, subunit beta, analysis of urease activation
gammaH96A
-
activity and nickel content are similar to wild-type enzyme
H219A
-
1000fold increased Km-value over that of the native enzyme
H219H
-
100fold increased Km-value over that of the native enzyme
H219Q
-
100fold increased Km-value over that of the native enzyme
H320A
-
100000fold deficiencies in rates, modest Km changes, disorders in the peptide flap covering their active sites, the pH-optimum is anomalous with optima near pH 6 and shoulders that extend to pH 9
H320N
-
100000fold deficiencies in rates, modest Km changes, disorders in the peptide flap covering their active sites, the pH-optimum is anomalous with optima near pH 6 and shoulders that extend to pH 9
H320Q
-
100000fold deficiencies in rates, modest Km changes, disorders in the peptide flap covering their active sites, the pH-optimum is anomalous with optima near pH 6 and shoulders that extend to pH 9
R336Q
-
0.0001fold decreased catalytic rate with near-normal pH dependence, unaffected Km-value, phenylglyoxal inactivates at over half the rate observed for the native enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
2 h, 30% loss of activity, wild-type enzyme
60
-
2 h, 55% loss of activity, wild-type enzyme. 2 h, complete inactivation of mutant enzymes betaH39A and alphaH320A
70
-
1 h, 87% loss of activity, wild-type enzyme, 58% loss of activity of mutant enzyme alphaG312A, complete inactivation of mutant enzymes gammaH96A, betaH39A, betaH41A, alphaH219A, alphaH320A and alphaH321A
additional information
-
Ni substantially increase stability of the intact metalloprotein, Tm = 79°C compared with apoenzyme Tm = 62°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant enzymes C319A, C319S, C319D and C319Y
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moncrief, M.B.C.; Hom, L.G.; Jabri, E.; Karplus, P.A.; Hausinger, R.P.
Urease activity in the crystalline state
Protein Sci.
4
2234-2236
1995
Klebsiella aerogenes
Manually annotated by BRENDA team
Pearson, M.A.; Park, I.S.; Schaller, R.A.; Michel, L.O.; Karplus, P.A.; Hausinger, R.P.
Kinetic and structural characterization of urease active site variants
Biochemistry
39
8575-8574
2000
Klebsiella aerogenes
Manually annotated by BRENDA team
Martin, P.R.; Hausinger, R.P.
Site-directed mutagenesis of the active site cysteine in Klebsiella aerogenes urease
J. Biochem.
267
20024-20027
1992
Klebsiella aerogenes
Manually annotated by BRENDA team
Park, I.S.; Hausinger, R.P.
Metal ion interactions with urease and UreD-urease apoproteins
Biochemistry
35
5352-5352
1996
Klebsiella aerogenes
Manually annotated by BRENDA team
Lee, M.H.; Mulrooney, S.B.; Hausinger, R.P.
Purification, characterization, and in vivo reconstitution of Klebsiella aerogenes urease apoenzyme
J. Bacteriol.
172
4427-4431
1990
Klebsiella aerogenes
Manually annotated by BRENDA team
Park, I.S.; Hausinger, R.P.
Site-directed mutagenesis of Klebsiella aerogenes urease: identification of histidine residues that appear to function in nickel ligation, substrate binding and catalysis
Protein Sci.
2
1034-1041
1993
Klebsiella aerogenes
Manually annotated by BRENDA team
Quiroz-Valenzuela, S.; Sukuru, S.C.; Hausinger, R.P.; Kuhn, L.A.; Heller, W.T.
The structure of urease activation complexes examined by flexibility analysis, mutagenesis, and small-angle X-ray scattering
Arch. Biochem. Biophys.
480
51-57
2008
Klebsiella aerogenes (P18314 and P18315 and P18316), Klebsiella aerogenes
Manually annotated by BRENDA team
Krajewska, B.
Ureases I. Functional, catalytic and kinetic properties: A review
J. Mol. Catal. B
59
9-21
2009
Klebsiella aerogenes, Pseudarthrobacter oxydans, Aspergillus nidulans, Aspergillus niger, Sporosarcina pasteurii, Corynebacterium ammoniagenes, Cajanus cajan, Canavalia ensiformis, Coccidioides immitis, Helicobacter pylori, Limosilactobacillus fermentum, Limosilactobacillus reuteri, Otala lactea, Proteus mirabilis, Providencia rettgeri, Providencia stuartii, Schizosaccharomyces pombe, Selenomonas ruminantium, Staphylococcus saprophyticus, Staphylococcus sp., Staphylococcus xylosus, Streptococcus mitior, Ureaplasma urealyticum, Staphylococcus leei, Brucella suis, Pseudomonas, Klebsiella, Arthrobacter mobilis, Nitellopsis obtusa
-
Manually annotated by BRENDA team
Farrugia, M.A.; Wang, B.; Feig, M.; Hausinger, R.P.
Mutational and computational evidence that a nickel-transfer tunnel in UreD is used for activation of Klebsiella aerogenes urease
Biochemistry
54
6392-6401
2015
Klebsiella aerogenes
Manually annotated by BRENDA team
Macomber, L.; Minkara, M.S.; Hausinger, R.P.; Merz, K.M.
Reduction of urease activity by interaction with the flap covering the active site
J. Chem. Inf. Model.
55
354-361
2015
Klebsiella aerogenes (P18314), Klebsiella aerogenes
Manually annotated by BRENDA team