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Information on EC 4.3.1.12 - ornithine cyclodeaminase and Organism(s) Pseudomonas putida and UniProt Accession Q88H32

for references in articles please use BRENDA:EC4.3.1.12
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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.12 ornithine cyclodeaminase
IUBMB Comments
Requires NAD+. The enzyme is a member of the mu-crystallin protein family . The reaction is stimulated by the presence of ADP or ATP and is inhibited by O2 .
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This record set is specific for:
Pseudomonas putida
UNIPROT: Q88H32
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas putida
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
ocd, ornithine cyclodeaminase, ornithine cyclase, atocd, ornithine cyclo-deaminase, ornithine cyclodeamidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyclase, ornithine (deaminating)
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deaminase, ornithine cyclo-
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ornithine cyclase
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ornithine cyclase (deaminating)
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ornithine cyclodeaminase
SYSTEMATIC NAME
IUBMB Comments
L-ornithine ammonia-lyase (cyclizing; L-proline-forming)
Requires NAD+. The enzyme is a member of the mu-crystallin protein family [4]. The reaction is stimulated by the presence of ADP or ATP and is inhibited by O2 [2].
CAS REGISTRY NUMBER
COMMENTARY hide
9054-76-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-ornithine
?
show the reaction diagram
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?
L-ornithine
L-proline + NH3
show the reaction diagram
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?
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
L-ornithine
?
show the reaction diagram
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?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method, crystal structure of the enzyme in complex with NADH, refined to 1.8 A resolution, crystal structure of crystals grown in presence of L-ornithine, refined to 1.6 A resolution
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vapor-diffusion method, the best diffraction-quality crystals are obtained from solutions of 40%(v/v) 2-methyl-2,4-pentanediol buffered at pH 6.0 with 0.1 M MES and diffracted X-rays to 1.68 A resolution. Crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 70.0, b = 78.3, c = 119.4 A
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in an ornithine overproducing platform strain with deletions of argR and argF (ORN1) from Corynebacterium glutamicum
expression in Escherichia coli XL-2-Blue
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
expression of ocd from Pseudomonas putida in an ornithine overproducing platform strain with deletions of argR and argF (ORN1) from Corynebacterium glutamicum results in proline production with yields up to 0.31 g proline/g glucose
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stalon, V.; Vander Wauven, C.; Momin, P.; Legrain, C.
Catabolism of arginine, citrulline and ornithine by Pseudomonas and related bacteria
J. Gen. Microbiol.
133
2487-2495
1987
Burkholderia cepacia, Acetoanaerobium sticklandii, Pseudomonas putida
Manually annotated by BRENDA team
Alam, S.; Wang, S.C.; Ruzicka, F.J.; Frey, P.A.; Wedekind, J.E.
Crystallization and X-ray diffraction analysis of ornithine cyclodeaminase from Pseudomonas putida
Acta Crystallogr. Sect. D
60
941-944
2004
Pseudomonas putida
Manually annotated by BRENDA team
Goodman, J.L.; Wang, S.; Alam, S.; Ruzicka, F.J.; Frey, P.A.; Wedekind, J.E.
Ornithine cyclodeaminase: structure, mechanism of action, and implications for the mu-crystallin family
Biochemistry
43
13883-13891
2004
Pseudomonas putida
Manually annotated by BRENDA team
Ion, B.F.; Bushnell, E.A.; Luna, P.D.; Gauld, J.W.
A molecular dynamics (MD) and quantum mechanics/molecular mechanics (QM/MM) study on ornithine cyclodeaminase (OCD): A tale of two iminiums
Int. J. Mol. Sci.
13
12994-13011
2012
Pseudomonas putida (Q88H32), Pseudomonas putida
Manually annotated by BRENDA team
Jensen, J.V.; Wendisch, V.F.
Ornithine cyclodeaminase-based proline production by Corynebacterium glutamicum
Microb. Cell Fact.
12
63
2013
Pseudomonas putida (Q88H32)
Manually annotated by BRENDA team