Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.5.3.22 - proclavaminate amidinohydrolase and Organism(s) Streptomyces clavuligerus and UniProt Accession P0DJQ3

for references in articles please use BRENDA:EC3.5.3.22
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
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+.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Streptomyces clavuligerus
UNIPROT: P0DJQ3
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Streptomyces clavuligerus
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
proclavaminate amidinohydrolase, proclavaminate amidino hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proclavaminate amidino hydrolase
proclavaminate amidinohydrolase
-
-
Proclavaminic acid amidino hydrolase
-
-
-
-
proclavaminic acid amidino hydrolaseproclavaminic acid amidino hydrolase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
amidinoproclavaminate + H2O = proclavaminate + urea
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-N bond
-
-
-
-
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+.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-96-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3R)-hydroxy-N-acetyl-L-arginine + H2O
?
show the reaction diagram
-
-
-
-
?
deoxyguanidinoproclavaminic acid + H2O
deoxyproclavaminic acid + urea
show the reaction diagram
guanidinoproclavaminic acid + H2O
proclavaminic acid + urea
show the reaction diagram
N-acetyl-L-arginine + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
guanidinoproclavaminic acid + H2O
proclavaminic acid + urea
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
preferred metal activator
Ni2+
-
50% of the activity with Co2+ as activator
additional information
-
no activation by Ca2+, Fe2+ and Zn2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12
(3R)-hydroxy-N-acetyl-L-arginine
-
pH 9.0, 37°C
30
N-acetyl-L-arginine
-
pH 9.0, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme is involved in clavulanic acid biosynthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PAH_STRCL
313
0
33401
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
199500
-
gel filtration
33000
-
x * 33000, SDS-PAGE
33300
-
x * 33300, deduced from gene sequence
33401
-
6 * 33401
34000
-
x * 34000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
-
6 * 33401
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
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°
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
overexpression as fusion to maltose-binding protein
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Streptomyces venezuelae
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
-
expressed in Streptomyces clavuligerus strain SMF5704
-
Streptomyces venezuelae YJ028 is utilized as the heterologous host for the expression of four structural clavulanic acid biosynthesis genes, which encode carboxyethylarginine synthase (ceas2), beta-lactam synthetase (bls2), clavaminate synthase (cas2), and proclavaminate amidinohydrolase (pah2). The genes are cloned into pIBR25 expression vector containing ermE promoter to generate pBS4. The cas2 gene is also cloned into pSET152 to generate pCas2. It is then integrated into the genome of Streptomyces venezuelae YJ028
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription of pah2 is increased in transformants over-expressing pah2
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
expression of four structural clavulanic acid biosynthesis genes, which encode carboxyethylarginine synthase (Ceas2), beta-lactam synthetase (Bls2), clavaminate synthase (Cas2), and proclavaminate amidinohydrolase (Pah2), in Streptomyces venezuelae enables production of clavulanic acid intermediates deoxygaunidinoproclavaminic acid, guanidinoproclavaminic acid, and dihydroclavaminic acid
synthesis
clavulanic acid intermediates: deoxygaunidinoproclavaminic acid, guanidinoproclavaminic acid, and dihydroclavaminic acid are heterologously produced in Streptomyces venezuelae recombinant using four sets of early genes from the clavulanic acid biosynthetic pathway
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wu, T.K.; Busby, R.W.; Houston, T.A.; McIlwaine, D.B.; Egan, L.A.; Townsend, C.A.
Identification, cloning, sequencing, and overexpression of the gene encoding proclavaminate amidino hydrolase and characterization of protein function in clavulanic acid biosynthesis
J. Bacteriol.
177
3714-3720
1995
Streptomyces clavuligerus
Manually annotated by BRENDA team
Jensen, S.E.; Paradkar, A.S.
Biosynthesis and molecular genetics of clavulanic acid
Antonie van Leeuwenhoek
75
125-133
1999
Streptomyces clavuligerus
Manually annotated by BRENDA team
Aidoo, K.A.; Wong, A.; Alexander, D.C.; Rittamer, R.A.R.; Jensen, S.E.
Cloning, sequencing and disruption of a gene from Streptomyces clavuligerus involved in clavulanic acid biosynthesis
Gene
147
41-46
1994
Streptomyces clavuligerus
Manually annotated by BRENDA team
Elson, S.W.; Baggaley, K.H.; Davison, M.; Fulston, M.; Nicholson, N.H.; Risbridger, G.D.; Tyler, J.W.
The identification of three new biosynthetic intermediates and one further biosynthetic enzyme in the clavulanic acid pathway
J. Chem. Soc. Chem. Commun.
1993
1212-1214
1993
Streptomyces clavuligerus
-
Manually annotated by BRENDA team
Elkins, J.M.; Clifton, I.J.; Hernandez, H.; Doan, L.X.; Robinson, C.V.; Schofield, C.J.; Hewitson, K.S.
Oligomeric structure of proclavaminic acid amidino hydrolase: evolution of a hydrolytic enzyme in clavulanic acid biosynthesis
Biochem. J.
366
423-434
2002
Streptomyces clavuligerus
Manually annotated by BRENDA team
Song, J.Y. ; Kim, E.S.; Kim, D.W.; Jensen, S.E.; Lee, K.J.
Functional effects of increased copy number of the gene encoding proclavaminate amidino hydrolase on clavulanic acid production in Streptomyces clavuligerus ATCC 27064
J. Microbiol. Biotechnol.
18
417-426
2008
Streptomyces clavuligerus
Manually annotated by BRENDA team
Jnawali, H.N.; Yoo, J.C.; Sohng, J.K.
Improvement of clavulanic acid production in Streptomyces clavuligerus by genetic manipulation of structural biosynthesis genes
Biotechnol. Lett.
33
1221-1226
2011
Streptomyces clavuligerus
Manually annotated by BRENDA team
Shrestha, B.; Dhakal, D.; Darsandhari, S.; Pandey, R.; Pokhrel, A.; Jnawali, H.; Sohng, J.
Heterologous production of clavulanic acid intermediates in Streptomyces venezuelae
Biotechnol. Bioprocess Eng.
22
359-365
2017
Streptomyces clavuligerus (B5GLC8), Streptomyces clavuligerus (P0DJQ3)
-
Manually annotated by BRENDA team