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Information on EC 4.3.1.2 - methylaspartate ammonia-lyase and Organism(s) Clostridium tetanomorphum and UniProt Accession Q05514
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4.3.1.2 methylaspartate ammonia-lyaseIUBMB Comments
A cobalamin protein.
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The taxonomic range for the selected organisms is: Clostridium tetanomorphum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
mal, 3-methylaspartase, 3-methylaspartate ammonia-lyase, 3-methylaspartate ammonia lyase, beta-methylaspartase, methylaspartate ammonia lyase, methylaspartate ammonia-lyase, ch-mal, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-methyl-L-aspartic acid ammonia-lyase
-
-
-
-
3-methylaspartase
-
-
-
-
3-methylaspartate ammonia-lyase
ammonia-lyase, methylaspartate
-
-
-
-
beta-methylaspartase
-
-
-
-
MAL
threo-3-methyl-L-aspartate ammonia-lyase
-
-
-
-
threo-3-methylaspartase ammonia-lyase
-
-
-
-
3-methylaspartate ammonia-lyase
-
-
-
-
MAL
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-threo-3-methylaspartate = mesaconate + NH3
mechanism
-
L-threo-3-methylaspartate = mesaconate + NH3
carbon mechanism
-
L-threo-3-methylaspartate = mesaconate + NH3
stereochemical mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -
SYSTEMATIC NAME
IUBMB Comments
L-threo-3-methylaspartate ammonia-lyase (mesaconate-forming)
A cobalamin protein.
CAS REGISTRY NUMBER
COMMENTARY
9033-26-5
-
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
(2E)-2-butylbut-2-enedioate + NH3
?
wild-type: conversion 0%, mutant L384A: conversion 59%
-
-
r
(2E)-2-ethylbut-2-enedioate + NH3
?
wild-type: conversion 74%, mutant L384A: conversion 76%
-
-
r
(2E)-2-hexylbut-2-enedioate + NH3
?
wild-type: conversion 0%, mutant L384A: conversion 53%
-
-
r
(2E)-2-methylbut-2-enedioate + NH3
?
wild-type: conversion 80%, mutant L384A: conversion 75%
-
-
r
(2E)-2-pentylbut-2-enedioate + NH3
?
wild-type: conversion 0%, mutant L384A: conversion 52%
-
-
r
(2E)-2-phenylbut-2-enedioate + NH3
?
wild-type: conversion 0%, mutant L384A: conversion 90%
-
-
r
(2E)-2-propylbut-2-enedioate + NH3
?
wild-type: conversion 57%, mutant L384A: conversion 67%
-
-
r
(2Z)-2-(benzyloxy)but-2-enedioate + NH3
?
wild-type: conversion 0%, mutant L384A: conversion 60%
-
-
r
(2Z)-2-(benzylsulfanyl)but-2-enedioate + NH3
?
wild-type: conversion 0%, mutant L384A: conversion 42%
-
-
r
(2Z)-2-(ethylsulfanyl)but-2-enedioate + NH3
?
wild-type: conversion 36%, mutant L384A: conversion 50%
-
-
r
(2Z)-2-(phenylsulfanyl)but-2-enedioate + NH3
?
wild-type: conversion 0%, mutant L384A: conversion 34%
-
-
r
(2Z)-2-ethoxybut-2-enedioate + NH3
?
wild-type: conversion 46%, mutant L384A: conversion 43%
-
-
r
(2Z)-2-phenoxybut-2-enedioate + NH3
?
wild-type: conversion 0%, mutant L384A: conversion 44%
-
-
r
L-threo-3-methylaspartic acid
mesaconate + NH3
assay at pH 9.0, 30°C
-
-
?
mesaconate + (aminooxy)ethane
?
mutant Q73A, conversion: 100%, yield: 61%
-
-
r
mesaconate + (aminooxy)methane
?
mutant Q73A, conversion: 99%, excess of threo isomer over erythro isomer: more than 95%
-
-
r
mesaconate + 2-aminoethanol
?
mutant Q73A, conversion: 37%, excess of threo isomer over erythro isomer: more than 95%
-
-
r
mesaconate + aniline
?
mutant Q73A, conversion: 6%, excess of threo isomer over erythro isomer: more than 95%
-
-
r
mesaconate + cyclohexanamine
?
mutant Q73A, conversion: 21%, excess of threo isomer over erythro isomer: more than 95%
-
-
r
mesaconate + cyclopentanamine
?
mutant Q73A, conversion: 36%, excess of threo isomer over erythro isomer: more than 95%
-
-
r
mesaconate + hexanamine
?
mutant Q73A, conversion: 17%, excess of threo isomer over erythro isomer: more than 95%
-
-
r
mesaconate + N-methylethane-1,2-diamine
?
mutant Q73A, conversion: 80%, excess of threo isomer over erythro isomer: more than 95%
-
-
r
mesaconate + NH3
L-threo-3-methylaspartate + L-erythro-3-methylaspartate
conversion 2h: 73% (wild-type), diastereomeric product ratio (threo:erythro) after 2h: 89:11
-
-
r
mesaconate + propan-2-amine
?
mutant Q73A, conversion: 8%, excess of threo isomer over erythro isomer: more than 95%, enantiomeric excess: more than 99%
-
-
r
mesaconic acid + NH3
L-threo-3-methylaspartate
assay at pH 9.0, 30°C
-
-
r
3-fluoroaspartate
fluorofumarate + NH3
-
-
not a good substrate
?
L-threo-3-methylaspartate
?
-
-
5670, 5997, 6049, 6050, 6051, 6053, 6054, 6055, 6056, 6057, 6058, 6059, 6060, 6062, 6064, 6065, 6066, 6067
-
-
?
L-threo-3-methylaspartate
mesaconate + NH3
the enzyme is part of a catabolic pathway for L-glutamate
-
-
?
mesaconate + 1-cyclopropylmethanamine
?
mutant Q73A, conversion: 61%, excess of threo isomer over erythro isomer: more than 95%, enantiomeric excess: more than 99%
-
-
r
mesaconate + 1-cyclopropylmethanamine
?
mutant Q73A, conversion: 96%, yield: 28%, enantiomeric excess: more than 99%
-
-
r
mesaconate + 2-methoxyethanamine
?
mutant Q73A, conversion: 100%, yield: 53%
-
-
r
mesaconate + 2-methoxyethanamine
?
mutant Q73A, conversion: 60%, excess of threo isomer over erythro isomer: more than 95%
-
-
r
mesaconate + 3-aminopropan-1-ol
?
mutant Q73A, conversion: 56%, excess of threo isomer over erythro isomer: 80%
-
-
r
mesaconate + 3-aminopropan-1-ol
?
mutant Q73A, conversion: 99%, yield: 57%
-
-
r
mesaconate + aminobutane
?
mutant Q73A, conversion: 60%, excess of threo isomer over erythro isomer: more than 95%, enantiomeric excess: more than 99%
-
-
r
mesaconate + aminobutane
?
mutant Q73A, conversion: 97%, yield: 33%, enantiomeric excess: more than 99%
-
-
r
mesaconate + cyclobutanamine
?
mutant Q73A, conversion: 65%, excess of threo isomer over erythro isomer: more than 95%, enantiomeric excess: more than 99%
-
-
r
mesaconate + cyclobutanamine
?
mutant Q73A, conversion: 99%, yield: 74%, enantiomeric excess: more than 99%
-
-
r
mesaconate + cyclopropanamine
?
mutant Q73A, conversion: 100%, yield: 48%
-
-
r
mesaconate + cyclopropanamine
?
mutant Q73A, conversion: 75%, excess of threo isomer over erythro isomer: more than 95%
-
-
r
mesaconate + ethanamine
?
mutant Q73A, conversion: 100%, yield: 75%, enantiomeric excess: more than 99%
-
-
r
mesaconate + ethanamine
?
mutant Q73A, conversion: 51%, excess of threo isomer over erythro isomer: more than 95%, enantiomeric excess: more than 99%
-
-
r
mesaconate + ethane-1,2-diamine
?
mutant Q73A, conversion: 90%, excess of threo isomer over erythro isomer: more than 95%
-
-
r
mesaconate + ethane-1,2-diamine
?
mutant Q73A, conversion: 99%, yield: 67%
-
-
r
mesaconate + methanamine
?
mutant Q73A, conversion: 100%, yield: 96%, enantiomeric excess: more than 99%
-
-
r
mesaconate + methanamine
?
mutant Q73A, conversion: 74%, excess of threo isomer over erythro isomer: more than 95%
-
-
r
mesaconate + NH3
L-threo-3-methylaspartate
mutant Q73A, conversion: 100%, yield: 79%, enantiomeric excess: more than 99%
-
-
r
mesaconate + NH3
L-threo-3-methylaspartate
mutant Q73A, conversion: 79%, excess of threo isomer over erythro isomer: 5%
-
-
r
mesaconate + NH3
L-threo-3-methylaspartate
wild-type: conversion 100%, mutant L384A: conversion 99%
-
-
r
mesaconate + pentanamine
?
mutant Q73A, conversion: 29%, excess of threo isomer over erythro isomer: more than 95%
-
-
r
mesaconate + pentanamine
?
mutant Q73A, conversion: 91%, yield: 14%, enantiomeric excess: more than 99%
-
-
r
mesaconate + propanamine
?
mutant Q73A, conversion: 53%, excess of threo isomer over erythro isomer: more than 95%, enantiomeric excess: more than 99%
-
-
r
mesaconate + propanamine
?
mutant Q73A, conversion: 99%, yield: 53%, enantiomeric excess: more than 99%
-
-
r
mesaconate + propane-1,3-diamine
?
mutant Q73A, conversion: 100%, yield: 61%
-
-
r
mesaconate + propane-1,3-diamine
?
mutant Q73A, conversion: 78%, excess of threo isomer over erythro isomer: more than 95%
-
-
r
3-bromoaspartate
bromofumarate + NH3
-
-
during reaction, enzyme becomes inactive. This is reduced in the presence of alternative substrates
?
erythro-3-methylaspartate
?
-
(2S,3R)-3-methylaspartic acid
-
-
?
L-aspartate
fumarate + NH3
-
rate of deamination 100 times slower than that of L-threo-3-methylaspartate
-
?
L-aspartate
fumarate + NH3
-
(2S,3R) [3-3H]aspartic acid
amination 1.8 times faster than the amination of mesaconate
?
L-aspartate
fumarate + NH3
-
(2S)-aspartate
amination 1.8 times faster than the amination of mesaconate
?
L-erythro-3-methylaspartate
mesaconate + NH3
-
i.e. (2S,3R)-3-methylaspartate, slow syn elimination
-
?
L-erythro-3-methylaspartate
mesaconate + NH3
-
i.e. (2S,3R)-3-methylaspartate, slow syn elimination
-
?, r
L-threo-3-methylaspartate
mesaconate + NH3
-
threo-beta-methyl-L-aspartate
-
?
L-threo-3-methylaspartate
mesaconate + NH3
-
threo-beta-methyl-L-aspartate
-
?
L-threo-3-methylaspartate
mesaconate + NH3
-
threo-beta-methyl-L-aspartate
-
?
L-threo-3-methylaspartate
mesaconate + NH3
-
beta-methylaspartate
-
?
L-threo-3-methylaspartate
mesaconate + NH3
-
(2S,3S)-3-methylaspartic acid
-
?
L-threo-3-methylaspartate
mesaconate + NH3
-
(2S,3S)-3-methylaspartic acid
-
?
L-threo-3-methylaspartate
mesaconate + NH3
-
(2S,3S)-3-methylaspartic acid
-
?
L-threo-3-methylaspartate
mesaconate + NH3
-
(2S,3S)-3-methylaspartic acid
-
?
L-threo-3-methylaspartate
mesaconate + NH3
-
(2S,3S)-3-methylaspartic acid
-
?
L-threo-3-methylaspartate
mesaconate + NH3
-
(2S,3S)-3-methylaspartic acid
-
?
L-threo-3-methylaspartate
mesaconate + NH3
-
(2S,3S)-3-methylaspartic acid
-
?
L-threo-3-methylaspartate
mesaconate + NH3
-
(2S,3S)-3-methylaspartic acid
-
?
L-threo-3-methylaspartate
mesaconate + NH3
-
(2S,3S)-3-methylaspartic acid
-
?
L-threo-3-methylaspartate
mesaconate + NH3
-
(2S,3S)-3-methylaspartic acid
-
?
L-threo-3-methylaspartate
mesaconate + NH3
-
(2S,3S)-3-methylaspartic acid
-
?
L-threo-3-methylaspartate
mesaconate + NH3
-
(2S,3S)-3-methylaspartic acid
-
?
L-threo-3-methylaspartate
mesaconate + NH3
-
i.e. (2S,3S)-3-methylaspartate
-
r
L-threo-3-methylaspartate
mesaconate + NH3
-
i.e. (2S,3S)-3-methylaspartate
-
r
additional information
?
-
-
enzyme is specific for the L-configuration
-
-
?
additional information
?
-
-
catalytic rates for the enzymatic amination of fumarate and mesaconate are faster than the rates of the corresponding deamination reactions
-
-
?
additional information
?
-
-
enzyme is involved in the catabolic pathway for glutamate
-
-
?
additional information
?
-
-
enzyme is involved in the catabolic pathway for glutamate
-
-
?
additional information
?
-
-
enzyme is associated with an anaerobic degradation of the (S)-glutamic acid in obligat anaerobes
-
-
?
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
L-threo-3-methylaspartate
mesaconate + NH3
the enzyme is part of a catabolic pathway for L-glutamate
-
-
?
L-erythro-3-methylaspartate
mesaconate + NH3
-
i.e. (2S,3R)-3-methylaspartate, slow syn elimination
-
r
L-threo-3-methylaspartate
?
-
-
5670, 5997, 6049, 6050, 6051, 6053, 6054, 6055, 6056, 6057, 6058, 6059, 6060, 6062, 6064, 6065, 6066, 6067
-
-
?
additional information
?
-
-
enzyme is involved in the catabolic pathway for glutamate
-
-
?
additional information
?
-
-
enzyme is involved in the catabolic pathway for glutamate
-
-
?
additional information
?
-
-
enzyme is associated with an anaerobic degradation of the (S)-glutamic acid in obligat anaerobes
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
K+
Mg2+
Mn2+
Ni2+
additional information
additional information
-
ionic radius plays an important part in determing the catalytic efficiency of divalent metal activators
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-ethylmaleimide
-
1 mM, complete inactivation after approx. 12 min
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
L-threo-3-methylaspartic acid
mutant K331A, value below 0.000001
additional information
mesaconic acid
mutant K331A, value below 0.000001
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme is part of a catabolic pathway for L-glutamate
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapour-diffusion, 0.0045 ml protein sample and 0.0045 ml precipitant, crystals are obtained using 20-25% polyethylene glycol 6000, 100 mM sodium acetate, pH 7.0, 25 mM Tris-HCl as precipitant solution and 16-22% ethylene glycol as additive, crystals diffract to 2.0 A
-
sitting-drop vapur diffusion against a well solution of 20-25% polyethylene glycol 6000, 100 mM sodium acetate, pH 7.0, 25 mM Tris-HCl pH 7.0 as precipitating solution and 16-22% ethylene glycol as additive, crystals diffract to 1.9 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C361A
kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 47% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)
C361K
mutant shows no reactivity. Conversion 2h: 10% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)
F170A
kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 63% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)
L384A
Q172A
kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 16% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)
Q172N
mutant shows no reactivity. Conversion 2h: 6% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)
Q73A
Q73N
mutant shows very low-level amination activity preventing the measurement of kinetic parameters. Conversion 2h: 18% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)
T360A
kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 38% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 93:7 (89:11 wild-type)
T360S
kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 76% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 86:14 (89:11 wild-type)
Y356A
kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 24% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)
L384A
kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 61% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)
L384A
mutant displays pronounced amination activity towards 2-hexylfumarate ad decreased amination activity towards mesaconate compared to wild-type. Mutant displays a broad electrophile scope including fumarate derivatives with alkyl, aryl, alkoxy, aryloxy, alkylthio and arylthio substituents at the C2 position
Q73A
analysis carried out with mutant Q73A. The potential of the mutant Q73A enzyme is shown for application in the asymmetric synthesis of a large variety of valuable N-substituted l-aspartic acids
Q73A
kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 37% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 91:9 (89:11 wild-type)
Q73A
mutant displays significant decrease in ammonia addition and a large increase in methylamine addition compared to wild-type. Mutant displays a wide nucleophile scope including structurally diverse linear and cyclic allkylamines
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-3°C, in 0.5 M tetramethylammonium chloride, pH 6.8 for many months, with little loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
starting from simple non-chiral dicarboxylic acids (either fumaric acid or mesaconic acid), vitamin B5 and both diastereoisomers of alpha-methyl-substituted vitamin B5, which are valuable precursors for promising antimicrobials against Plasmodium falciparum and multidrug-resistant Staphylococcus aureus, can be generated in good yields (up to 70%) and excellent enantiopurity (>99% ee). Access to vitamin B5 ((R)-pantothenic acid) and both diastereoisomers of alpha-methyl-substituted vitamin B5 ((R)- and (S)-3-((R)-2,4-dihydroxy-3,3-dimethylbutanamido)-2-methylpropanoic acid) is achieved using a modular three-step biocatalytic cascade involving 3-methylaspartate ammonia lyase (MAL), aspartate-a-decarboxylase (ADC), beta-methylaspartate-alpha-decarboxylase (CrpG) or glutamate decarboxylase (GAD), and pantothenate synthetase (PS) enzymes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kato, Y.; Asano, Y.
3-Methylaspartate ammonia-lyase as a marker enzyme of the mesaconate pathway for (S)-glutamate fermentation in Enterobacteriaceae
Arch. Microbiol.
168
457-463
1997
Citrobacter amalonaticus, Citrobacter amalonaticus YG-1002, Citrobacter freundii, Citrobacter freundii TPU 0011, Citrobacter freundii YG-0504, Citrobacter koseri, Citrobacter koseri JCM 1658, Citrobacter koseri JCM 1659, Clostridium tetanomorphum, Morganella morganii, Morganella morganii NCIMB 10466, Morganella morganii NCIMB 232, Morganella morganii NCIMB 9525, Morganella morganii YG-0601, Raoultella planticola, Raoultella planticola IAM 1133
Hanson, K.R.; Havir, E.A.
The enzymic elimination of ammonia
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
7
75-166
1972
Bacterium cadaveris, Clostridium tetanomorphum, Clostridium tetanomorphum H1 / ATCC 15920
-
Bright, H.J.; Ingraham, L.L.
The preparation of crystalline beta-methylaspartase
Biochim. Biophys. Acta
44
586-588
1960
Clostridium tetanomorphum
-
Bright, H.J.
Divalent metal activation of beta-methylaspartase. The importance of ionic radius
Biochemistry
6
1191-1203
1967
Clostridium tetanomorphum
Hsiang, M.W.; Bright, H.J.
beta-methylaspartase from Clostridium tetanomorphum
Methods Enzymol.
13
347-353
1969
Bacterium cadaveris, Clostridium tetanomorphum, Clostridium tetanomorphum H1 / ATCC 15920
-
Akhtar, M.; Cohen, M.A.; Gani, D.
Enzymic synthesis of 3-halogenoaspartic acids using beta-methylaspartase: Inhibition by 3-bromoaspartic acid
J. Chem. Soc. Chem. Commun.
1986
1290-1291
1980
Clostridium tetanomorphum
-
Akhtar, M.; Botting, N.P.; Cohen, M.A.; Gani, D.
Enantiospecific synthesis of 3-substituted aspartic acids via enzymic amination of substituted fumaric acids
Tetrahedron
43
5899-5908
1987
Clostridium tetanomorphum
-
Botting, N.P.; Akhtar, M.; Cohen, M.A.; Gani, D.
Substrate specificity of the 3-methylaspartate ammonia-lyase reaction: Observation of differential relative reaction rates for substrate-product pairs
Biochemistry
27
2953-2955
1988
Clostridium tetanomorphum, Clostridium tetanomorphum H1 / ATCC 15920
Botting, N.P.; Cohen, M.A.; Akhtar, M.; Gani, D.
Primary deuterium isotope effects for the 3-methylaspartase-catalyzed deamination of (2S)-aspartic acid, (2S,3S)-3-methylaspartic acid, and (2S,3S)-3-ethylaspartic acid
Biochemistry
27
2956-2959
1988
Clostridium tetanomorphum, Clostridium tetanomorphum H1 / ATCC 15920
Goda, S.K.; Minton, N.P.; Botting, N.P.; Gani, D.
Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein
Biochemistry
31
10747-10756
1992
Clostridium tetanomorphum, Clostridium tetanomorphum H1 / ATCC 15920
Botting, N.P.; Gani, D.
Mechanism of C-3 hydrogen exchange and the elimination of ammonia in the 3-methylaspartate ammonia-lyase reaction
Biochemistry
31
1509-1520
1992
Clostridium tetanomorphum, Clostridium tetanomorphum H1 / ATCC 15920
Kato, Y.; Asano, Y.
3-Methylaspartate ammonia-lyase from a facultative anaerobe, strain YG-1002
Appl. Microbiol. Biotechnol.
43
901-907
1995
Citrobacter amalonaticus, Clostridium tetanomorphum, Citrobacter amalonaticus YG-1002, Clostridium tetanomorphum H1 / ATCC 15920, Clostridium tetanomorphum NCIMB 11547
Kato, Y.; Asano, Y.
Purification and properties of crystalline 3-methylaspartase from two facultative anaerobes, Citrobacter sp. strain YG-0504 and Morganella morganii strain YG-0601
Biosci. Biotechnol. Biochem.
59
93-99
1995
Citrobacter freundii, Clostridium tetanomorphum, Morganella morganii, Clostridium tetanomorphum NCIMB 11547, Morganella morganii YG-0601
Kato, Y.; Asano, Y.
Cloning, nucleotide sequencing, and expression of the 3-methylaspartate ammonia-lyase gene from Citrobacter amalonaticus strain YG-1002
Appl. Microbiol. Biotechnol.
50
468-474
1998
Citrobacter amalonaticus, Clostridium tetanomorphum, Citrobacter amalonaticus YG-1002, Citrobacter amalonaticus TPU 6323, Clostridium tetanomorphum NCIMB 11547
Gani, D.; Archer, C.H.; Botting, N.P.; Pollard, J.R.
The methylaspartase reaction probed using 2H- and 15N-isotope E ects for three substrates: A flip from a concerted to a carbocationic amino-enzyme elimination mechanism upon changing the C-3 stereochemistry in the substrate from R to S
Bioorg. Med. Chem.
7
977-990
1999
Clostridium tetanomorphum, Clostridium tetanomorphum H1 / ATCC 15920
Winkler, M.F.; Williams, V.R.
New substrates for beta-methylaspartase
Biochim. Biophys. Acta
146
287-289
1967
Clostridium tetanomorphum
Botting, N.P.; Akhtar, M.; Cohen, M.A.; Gani, D.
Mechanism of the enzymic elimination of ammonia from 3-substituted aspartic acids by 3-methylaspartase
J. Chem. Soc. Chem. Commun.
1987
1371-1373
1987
Bacterium cadaveris, Clostridium tetanomorphum
-
Akhtar, M.; Cohen, M.A.; Gani, D.
Stereochemical course of the enzymic amination of chloro- and bromo acid by 3-methylaspartate ammoni-lyase
Tetrahedron Lett.
28
2413-2416
1987
Bacterium cadaveris, Clostridium tetanomorphum
-
Asuncion, M.; Barlow, J.N.; Pollard, J.; Staines, A.G.; McMahon, S.A.; Blankenfeldt, W.; Gani, D.; Naismith, J.H.
Overexpression, purification, crystallization and data collection of 3-methylaspartase from Clostridium tetanomorphum
Acta Crystallogr. Sect. D
57
731-733
2001
Clostridium tetanomorphum
Pollard, J.R.; Richardson, S.; Akhtar, M.; Lasry, P.; Neal, T.; Botting, N.P.; Gani, D.
Mechanism of 3-methylaspartase probed using deuterium and solvent isotope effects and active-site directed reagents: identification of an essential cysteine residue
Bioorg. Med. Chem.
7
949-975
1999
Clostridium tetanomorphum, Clostridium tetanomorphum H1 / ATCC 15920
Asuncion, M.; Blankenfeldt, W.; Barlow, J.N.; Gani, D.; Naismith, J.H.
The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step
J. Biol. Chem.
277
8306-8311
2002
Clostridium tetanomorphum
Asano, Y.; Kato, Y.; Levy, C.; Baker, P.; Rice, D.
Structure and Function of Amino Acid Ammonia-lyases
Biocatal. Biotransform.
22
131-138
2004
Citrobacter amalonaticus, Citrobacter freundii, Clostridium tetanomorphum, Morganella morganii, Citrobacter amalonaticus YG-1002, Clostridium tetanomorphum H1 / ATCC 15920, Citrobacter freundii YG.0504, Morganella morganii YG-0601
-
Raj, H.; Weiner, B.; Veetil, V.P.; Reis, C.R.; Quax, W.J.; Janssen, D.B.; Feringa, B.L.; Poelarends, G.J.
Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis
ChemBioChem
10
2236-2245
2009
Clostridium tetanomorphum (Q05514)
PuthanVeetil, V.; Raj, H.; DeVilliers, M.; Tepper, P.; Dekker, F.; Quax, W.; Poelarends, G.
Enantioselective Synthesis of N-Substituted Aspartic Acids Using an Engineered Variant of Methylaspartate Ammonia Lyase
ChemCatChem
5
1325-1327
2013
Clostridium tetanomorphum (Q05514)
-
Raj, H.; Poelarends, G.J.
The roles of active site residues in the catalytic mechanism of methylaspartate ammonia-lyase
FEBS open bio
3
285-290
2013
Clostridium tetanomorphum (Q05514), Clostridium tetanomorphum
Raj, H.; Szymanski, W.; de Villiers, J.; Rozeboom, H.J.; Veetil, V.P.; Reis, C.R.; de Villiers, M.; Dekker, F.J.; de Wildeman, S.; Quax, W.J.; Thunnissen, A.M.; Feringa, B.L.; Janssen, D.B.; Poelarends, G.J.
Engineering methylaspartate ammonia lyase for the asymmetric synthesis of unnatural amino acids
Nat. Chem.
4
478-484
2012
Clostridium tetanomorphum (Q05514)
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