PMID- 7858967
OWN - NLM
STAT- MEDLINE
DCOM- 19950320
LR  - 20190830
IS  - 0968-0896 (Print)
IS  - 0968-0896 (Linking)
VI  - 2
IP  - 7
DP  - 1994 Jul
TI  - An enzymatic route to L-ornithine from arginine--activation, selectivity and 
      stabilization of L-arginase.
PG  - 617-26
AB  - The non-proteinogenic amino acid L-ornithine (L-Orn) can be conveniently obtained 
      by enzymatic hydrolysis of arginine (Arg) with arginase (EC 3.5.3.1). Arginase 
      from calf liver (Vmax = 459 mumol/(min.mg), Km = 25.5 mM) is inhibited 
      competitively by L-Orn (Ki = 480 mM). The enzyme was found to be completely 
      enantioselective (E-value > 100) so that D,L-Arg can be split into D-Arg and 
      L-Orn. Operational stability at 25 degrees C (deactivation rate constant kdeact = 
      3.8 x 10(-3) h-1; tau 1/2 = 182 h) is sufficient for use in a continuous process 
      but is significantly smaller than temperature stability (kdeact = 4.1 x 10(-4) 
      h-1; tau 1/2 = 1682 h); mechanical stress through stirring and unsteady Mn2+ 
      supply owing to oxidation in the continuous process are believed to cause the 
      difference. Addition of ascorbic acid stabilizes calf liver arginase at 
      temperatures higher than 25 degrees C (at 60 degrees C, delta delta G not equal 
      to = 2.9 kJ/mol).
FAU - Bommarius, A S
AU  - Bommarius AS
AD  - DEGUSSA AG, Organic and Biological Chemistry R&D, Hanau, Germany.
FAU - Drauz, K
AU  - Drauz K
LA  - eng
PT  - Journal Article
PL  - England
TA  - Bioorg Med Chem
JT  - Bioorganic & medicinal chemistry
JID - 9413298
RN  - 94ZLA3W45F (Arginine)
RN  - E524N2IXA3 (Ornithine)
RN  - EC 3.5.3.1 (Arginase)
SB  - IM
MH  - Animals
MH  - Arginase/antagonists & inhibitors/chemistry/*metabolism
MH  - Arginine/chemistry/*metabolism
MH  - Cattle
MH  - Enzyme Activation
MH  - Enzyme Stability
MH  - Hydrogen-Ion Concentration
MH  - Kinetics
MH  - Liver/*enzymology
MH  - Molecular Structure
MH  - Ornithine/chemistry/*metabolism/pharmacology
MH  - Regression Analysis
MH  - Stereoisomerism
MH  - Substrate Specificity
EDAT- 1994/07/01 00:00
MHDA- 1994/07/01 00:01
CRDT- 1994/07/01 00:00
PHST- 1994/07/01 00:00 [pubmed]
PHST- 1994/07/01 00:01 [medline]
PHST- 1994/07/01 00:00 [entrez]
AID - 0968-0896(94)85009-7 [pii]
AID - 10.1016/0968-0896(94)85009-7 [doi]
PST - ppublish
SO  - Bioorg Med Chem. 1994 Jul;2(7):617-26. doi: 10.1016/0968-0896(94)85009-7.