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Information on EC 3.5.1.86 - mandelamide amidase
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3.5.1.86 mandelamide amidaseSpecify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
amidase, mandelamide, MAH, mandelamide hydrolase, Pseudomonas mandelamide hydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
amidase, mandelamide
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-
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MAH
mandelamide hydrolase
Pseudomonas mandelamide hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-mandelamide + H2O = (R)-mandelate + NH3
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of amide bond
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
mandelamide hydrolase
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CAS REGISTRY NUMBER
COMMENTARY
198496-85-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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the lack of reactivity of MAH with the corresponding ethyl ester confirms the very limited size of the MAH leaving group site. The reactivity of MAH with 4-nitrophenyl acetate and methyl 4-nitrophenyl carbonate, therefore, suggests formation of an inverse acyl-enzyme where the small acyl-group occupies the normal leaving group site. Both (R)- and (S)-mandelamide are excellent substrates for MAH, while the enzyme can hydrolyze phenylacetamide with even higher catalytic efficiency. Reaction scheme for interaction of substrates with MAH. Substrate specificity, overview. No activity with ethyl 4-nitrophenylacetate, phenyl carbamate, and N-benzyloxycarbonyl-glycinamide, poor activity with phenyl acetate, 4-nitrophenyl n-butyrate, and ethyl 4-nitrophenyl carbonate
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phenylmethylboronic acid
a potent inhibitor of enzyme MAH that forms a transition state analogue structure with the enzyme
additional information
O-acyl hydroxamates are no irreversible inactivators of MAH but some are found to be transient inhibitors. Reactivity of MAH with some recently studied beta-lactamase inhibitors, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the catalytic triad of MAH is composed of Ser204, Ser180, and Lys100. Modeling of substrate binding. A model of the deacylation tetrahedral intermediate is derived from reaction of MAH with phenylacetamide, overview
Show AA Sequence and Transmembrane Helices (324 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
53820
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S204A
S180A
F150L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type
K100A
G202V
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site-directed mutagenesis. Reduction in activity increases to six orders of magnitude for the G202V variant
G202A
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site-directed mutagenesis. Gly202 appears to control the preference for aromatic substrates as the G202A variant shows three orders of magnitude decrease in kcat/Km for (R)- and (S)-mandelamide
F433L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type
F433A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type
S204A
site-directed mutagenesis, mutation of a catalytic residue, inactive mutant
S180A
site-directed mutagenesis, mutation of a catalytic residue, 4200fold decrease in the kcat/Km value
K100A
site-directed mutagenesis, mutation of a catalytic residue, inactive mutant
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, phosphate buffer pH 7.8, 1 mM EDTA, stable for at least 1 month
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
Sephacryl S-200 gel filtration, HiPrep Q anion-exchange column chromatography, and HiTrap Q column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli both wild type and His6-tagged protein
recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yamamoto, K.; Oishi, K.; Fujimatsu, I.; Komatsu, K.
Production of R-(-)-mandelic acid from mandelonitrile by Alcaligenes faecalis ATCC 8750
Appl. Environ. Microbiol.
57
3028-3032
1991
Alcaligenes faecalis, Brevundimonas vesicularis, Corynebacterium nitrilophilus, Corynebacterium sp., Corynebacterium sp. C5, Meyerozyma guilliermondii, Mycobacterium sp., Mycobacterium sp. AC777, Rhodococcus sp., Rhodococcus sp. AK32
brenda
Kooo, C.W.
Mandelamide hydrolase from Pseudomonas putida
Diss. Abstr. Int. B
58
1865
1997
Pseudomonas putida
-
brenda
Gopalakrishna, K.N.; Stewart, B.H.; Kneen, M.M.; Andricopulo, A.D.; Kenyon, G.L.; McLeish, M.J.
Mandelamide hydrolase from Pseudomonas putida: characterization of a new member of the amidase signature family
Biochemistry
43
7725-7735
2004
Pseudomonas putida (Q84DC4), Pseudomonas putida
brenda
McLeish, M.J.; Kneen, M.M.; Gopalakrishna, K.N.; Koo, C.W.; Babbitt, P.C.; Gerlt, J.A.; Kenyon, G.L.
Identification and characterization of a mandelamide hydrolase and an NAD(P)+dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633
J. Bacteriol.
185
2451-2456
2003
Pseudomonas putida
brenda
Wang, P.F.; Yep, A.; Kenyon, G.L.; McLeish, M.J.
Using directed evolution to probe the substrate specificity of mandelamide hydrolase
Protein Eng. Des. Sel.
22
103-110
2009
Pseudomonas putida
brenda
Adediran, S.A.; Wang, P.F.; Shilabin, A.G.; Baron, C.A.; McLeish, M.J.; Pratt, R.F.
Specificity and mechanism of mandelamide hydrolase catalysis
Arch. Biochem. Biophys.
618
23-31
2017
Pseudomonas putida (Q84DC4)
brenda
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