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Information on EC 4.1.3.41 - 3-hydroxy-D-aspartate aldolase for references in articles please use BRENDA:EC4.1.3.41Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Paracoccus denitrificans
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3-hydroxy-D-aspartate aldolase
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D-erythro-3-hydroxyaspartate = glycine + glyoxylate
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threo-3-hydroxy-D-aspartate = glycine + glyoxylate
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3-hydroxy-D-aspartate glyoxylate-lyase (glycine-forming)
A pyridoxal-phosphate protein. The enzyme, purified from the bacterium Paracoccus denitrificans IFO 13301, is strictly D-specific as to the alpha-position of the substrate, but accepts both the threo and erythro forms at the beta-position. The erythro form is a far better substrate (about 100-fold). The enzyme can also accept D-allothreonine, D-threonine, erythro-3-phenyl-D-serine and threo-3-phenyl-D-serine. Different from EC 4.1.3.14, erythro-3-hydroxy-L-aspartate aldolase. Requires a divalent cation, such as Mg2+, Mn2+ or Co2+.
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D-3-hydroxyaspartate aldolase
D-3-hydroxyaspartate aldolase
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D-3-hydroxyaspartate aldolase
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strain IFO 13301
UniProt
brenda
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2-amino-3-hydroxybutanedioic acid
aminoacetic acid + oxoacetic acid
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r
D-3-3,4-dihydroxyphenylserine
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D-erythro-3-3,4-methylenedioxyphenylserine
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D-erythro-3-hydroxyaspartate
glycine + glyoxylate
the enzyme is strictly D-specific as to the alpha-position, whereas it does not distinguish between threo and erythro forms at the beta-position
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D-erythro-3-phenylserine
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D-threo-3-3,4-methylenedioxyphenylserine
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D-threo-3-phenylserine
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additional information
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the enzyme shows no activity towards L-erythro-3-hydroxyaspartate, L-threo-3-hydroxyaspartate, L-threonine, L-allo-threonine, L-erythro-3-phenylserine, L-threo-3-phenylserine, L-erythro-3-3,4-methylenedioxyphenylserine, and L-threo-3-3,4-methylenedioxyphenylserine
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Co2+
2.0fold increase of specific activity in the presence of 1 mM Co2+
Mg2+
5.4fold increase of specific activity in the presence of 1 mM Mg2+
Mn2+
8.1fold increase of specific activity in the presence of 1 mM Mn2+
additional information
K+ and Na+ do not have an effect on the enzymatic activity
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EDTA
82% inhibition at 1 mM
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0.4
D-erythro-3-hydroxyaspartate
in 0.02 mM HEPES buffer, pH 8.0, at 30°C
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0.36
after 50fold purification, using DL-threo-3-hydroxyaspartate as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C
0.6
crude extract, in 0.02 mM HEPES buffer, pH 8.0, at 30°C
14.6
after 50fold purification, using D-threo-3-3,4-methylenedioxyphenylserine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C
17.5
after 50fold purification, using D-erythro-3-3,4-methylenedioxyphenylserine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C
20
after 50fold purification, using D-threonine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C
25
after 50fold purification, using D-allo-threonine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C
30
after 50fold purification, using D-erythro-3-hydroxyaspartate as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C
95
after 50fold purification, using D-threo-3-phenylserine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C
99
after 50fold purification, using D-erythro-3-phenylserine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C
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41633
2 * 41633, calculated from amino acid sequence
43000
2 * 43000, SDS-PAGE
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homodimer
2 * 41633, calculated from amino acid sequence; 2 * 43000, SDS-PAGE
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6.5 - 8.5
the enzyme is stable between pH 6.5 and 8.5 for 30 min at 30°C
649407
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45
the enzyme retains 50% activity upon heating at 45°C for 30 min
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ammonium sulfate fractionation, hydroxyapatite column chromatography, DEAE-Toyopearl column chromatography, phenyl-Toyopearl column chromatography, Superdex 200 gel filtration, and Mono Q column chromatography
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expressed in Escherichia coli XL1-Blue MRF cells
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DHAA_PARDE
387
41633
Swiss-Prot
A0A1Q9NQB5_9ARCH
400
45221
TrEMBL
A0A168F2W3_9MICO
379
39529
TrEMBL
A0A0M6ZUD0_9RHOB
387
41512
TrEMBL
A0A238KYB4_9RHOB
387
42011
TrEMBL
A0A1Y5RSD5_9RHOB
387
41731
TrEMBL
A0A165UXS6_9RHOB
383
41591
TrEMBL
A0A1X6YSV6_9RHOB
387
41050
TrEMBL
A0A158AZ95_9BURK
363
39624
TrEMBL
A0A2R8ANR6_9RHOB
381
39812
TrEMBL
A0A1Y0EDV4_9RHOB
388
41753
TrEMBL
A0A075R191_BRELA
437
49317
TrEMBL
A0A0U5LDT1_STRRE
400
42625
TrEMBL
A0A2S5CYW4_LYSSH
391
43788
TrEMBL
A0A1X6YIB9_9RHOB
387
41911
TrEMBL
A0A1X6ZHW5_9RHOB
387
41194
TrEMBL
A0A173KSP3_9SPHN
394
41723
TrEMBL
A0A1X6ZMG2_9RHOB
387
41434
TrEMBL
A0A1X6Z133_9RHOB
387
41496
TrEMBL
A0A2K8R0U5_9ACTN
398
43006
TrEMBL
A0A0M6Z054_9RHOB
387
41684
TrEMBL
A0A177HMF7_9ACTN
400
42956
TrEMBL
A0A238KR64_9RHOB
388
41961
TrEMBL
A0A166E1M3_9RHOB
383
41542
TrEMBL
A0A0K0Y218_9RHOB
387
41828
TrEMBL
A0A0M6Y531_9RHOB
387
42005
TrEMBL
A0A1Y5T2G3_9RHOB
387
41311
TrEMBL
A0A1X7BL17_9RHOB
387
41657
TrEMBL
A0A0M9EIN2_9RHOB
384
40999
TrEMBL
A0A165XP89_9RHOB
383
41574
TrEMBL
A0A2P8A1T7_9ACTN
402
42376
TrEMBL
A0A1S6HL89_9GAMM
382
41471
TrEMBL
A0A0B0H988_SOVGS
385
41977
TrEMBL
A0A1Y5RCQ8_9RHOB
387
41642
TrEMBL
A0A1B9EU73_9ACTN
400
42617
TrEMBL
A0A1V0RPL7_9RHOB
387
41747
TrEMBL
A0A0P1I1T8_9RHOB
387
41984
TrEMBL
A0A0L6CU14_9RHOB
269
28825
TrEMBL
A0A1S7RXS2_9RHIZ
387
41966
TrEMBL
A0A0S3PRE8_9BRAD
373
39554
TrEMBL
A0A2N9MTF0_9BACT
413
45378
TrEMBL
A0A0P8AJ35_9RHOB
387
41742
TrEMBL
A0A165SMY0_9RHOB
383
41512
TrEMBL
A0A0M6XME9_9RHOB
386
41847
TrEMBL
A0A2S6X5X7_9ACTN
402
42540
TrEMBL
A0A1X7A6H6_9RHOB
387
41809
TrEMBL
A0A1Y0EI49_9RHOB
387
41970
TrEMBL
A0A0P1E975_9RHOB
387
41943
TrEMBL
A0A2N9BI62_STRCX
400
42159
TrEMBL
A0A1Y0E8F1_9RHOB
387
41626
TrEMBL
A0A0D1CQ50_9RHOB
372
39651
TrEMBL
A0A2R8B4F7_9RHOB
387
42003
TrEMBL
A0A142XUD3_9PLAN
396
42998
TrEMBL
A0A1J5QIN7_9ZZZZ
385
40725
TrEMBL
A0A1X6Y8G2_9RHOB
388
41791
TrEMBL
A0A2P4UM41_9ACTN
400
42260
TrEMBL
A0A0B0HVZ4_9BACL
194
21817
TrEMBL
A0A0F0LMS5_9MICO
422
44404
TrEMBL
A0A2R8ALR8_9RHOB
387
41658
TrEMBL
A0A2N7QXN7_9GAMM
385
41771
TrEMBL
A0A238J338_9RHOB
387
41561
TrEMBL
A0A100JC27_9ACTN
400
43034
TrEMBL
A0A0P1EAY3_9RHOB
387
41862
TrEMBL
A0A090ENL5_9RHIZ
369
39491
TrEMBL
A0A238L4Z5_9RHOB
387
41469
TrEMBL
A0A1L9NU80_9RHOB
387
41371
TrEMBL
A0A2S0XE22_9RHIZ
387
41554
TrEMBL
A0A1S7TH73_RHIRD
398
43192
TrEMBL
A0A1Y5SSM6_9RHOB
387
41981
TrEMBL
A0A0P1FQK4_9RHOB
387
41676
TrEMBL
A0A2R8C6V1_9RHOB
387
41329
TrEMBL
A0A0H4LG47_9RHOB
387
41725
TrEMBL
A0A100JRQ8_STRSC
400
42626
TrEMBL
A0A2R8BPU4_9RHOB
387
41928
TrEMBL
A0A238LF34_9RHOB
386
41502
TrEMBL
A0A222E9Q7_9RHOB
387
41584
TrEMBL
A0A221K6G8_9RHOB
387
41619
TrEMBL
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Liu, J.Q.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.
A novel enzyme, D-3-hydroxyaspartate aldolase from Paracoccus denitrificans IFO 13301: purification, characterization, and gene cloning
Appl. Microbiol. Biotechnol.
62
53-60
2003
Paracoccus denitrificans (Q8GRC8)
brenda
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