Information on EC 3.5.3.22 - proclavaminate amidinohydrolase

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The expected taxonomic range for this enzyme is: Streptomyces clavuligerus

EC NUMBER
COMMENTARY
3.5.3.22
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RECOMMENDED NAME
GeneOntology No.
proclavaminate amidinohydrolase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
amidinoproclavaminate + H2O = proclavaminate + urea
show the reaction diagram
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amidinoproclavaminate + H2O = proclavaminate + urea
show the reaction diagram
forms part of the pathway for the biosynthesis of the beta-lactamase inhibitor clavulanate in Streptomyces clavuligerus, it carries out an intermediary reaction between the first reaction of EC 1.14.11.21, clavaminate synthase, and the second and third reactions of that enzyme, overview
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amidinoproclavaminate + H2O = proclavaminate + urea
show the reaction diagram
mechanism
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REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of C-N bond
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-
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PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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clavulanate biosynthesis
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Clavulanic acid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
amidinoproclavaminate amidinohydrolase
Forms part of the pathway for the biosythesis of the beta-lactamase inhibitor clavulanate in Streptomyces clavuligerus. It carries out an intermediary reaction between the first reaction of EC 1.14.11.21, clavaminate synthase, and the second and third reactions of that enzyme. Requires Mn2+.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
PAH
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-
-
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proclavaminate amidino hydrolase
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proclavaminate amidino hydrolase
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proclavaminate amidinohydrolase
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Proclavaminic acid amidino hydrolase
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proclavaminic acid amidino hydrolaseproclavaminic acid amidino hydrolase
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CAS REGISTRY NUMBER
COMMENTARY
9000-96-8
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain ATCC 27064
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3R)-hydroxy-N-acetyl-L-arginine + H2O
?
show the reaction diagram
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-
-
-
?
deoxyguanidinoproclavaminic acid + H2O
deoxyproclavaminic acid + urea
show the reaction diagram
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-
-
?
deoxyguanidinoproclavaminic acid + H2O
deoxyproclavaminic acid + urea
show the reaction diagram
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hydrolyzed much less rapidly than guanidinoproclavamic acid
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-
?
guanidinoproclavaminic acid + H2O
proclavaminic acid + urea
show the reaction diagram
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-
-
-
?
guanidinoproclavaminic acid + H2O
proclavaminic acid + urea
show the reaction diagram
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best substrate
-
?
guanidinoproclavaminic acid + H2O
proclavaminic acid + urea
show the reaction diagram
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best substrate, i.e. 3-hydroxy-5-guanidino-2-(2-oxoazetidin-1-yl)pentanoic acid, probably 2S,3R enantiomer
natural product is 2S,3R enantiomer
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N-acetyl-L-arginine + H2O
?
show the reaction diagram
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-
-
-
?
guanidinoproclavaminic acid + H2O
proclavaminic acid + urea
show the reaction diagram
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involved in clavulanic acid biosynthesis
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-
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additional information
?
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no substrate inhibition observed, no substrate: D-arginine, L-arginine, N-acetyl-L-arginine
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additional information
?
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no substrate: arginine
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additional information
?
-
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no detectable arginase activity
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
guanidinoproclavaminic acid + H2O
proclavaminic acid + urea
show the reaction diagram
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involved in clavulanic acid biosynthesis
-
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METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
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preferred metal activator
Mn2+
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enhances activity
Ni2+
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50% of the activity with Co2+ as activator
Mn2+
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50% of the activity with Co2+ as activator
additional information
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no activation by Ca2+, Fe2+ and Zn2+
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
12
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(3R)-hydroxy-N-acetyl-L-arginine
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pH 9.0, 37°C
30
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N-acetyl-L-arginine
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pH 9.0, 37°C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
199500
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gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
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x * 34000, SDS-PAGE
?
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x * 33300, deduced from gene sequence
?
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x * 33000, SDS-PAGE
hexamer
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6 * 33401
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging-drop vapour-diffusion method, crystal structures of the enzyme at 1.75 A and 2.45 A resolution. Crystals belong to space group P2(1), with unit cell dimensions a = 95.4 A, b = 81.9 A, c = 118.6 A beta = 95.5°, but following transfer into the sucrose solution they belong to C2, with unit cell dimensions a = 140.0 A, b = 79.0 A, c = 93.5 A and beta = 124.0°
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
amplified from Streptomyces clavuligerus genomic DNA. Cloned in the pSET152 integration and pIBR25 expression vectors containing the strong ermE promoter. Plasmids are introduced into Streptomyces clavuligerus by protoplast transformation
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expressed in Streptomyces clavuligerus strain SMF5704
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EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
transcription of pah2 is increased in transformants over-expressing pah2
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
overexpression as fusion to maltose-binding protein